Biochemistry PDF

2
Biyani's Think Tank

Concept based notes
Biochemistry-I
(B.Sc. Biotechnology Part-I)
Juhi Saxena
Revised by: Dr. Leena Kansal
Lecturer
Deptt. of Science
Biyani Girls College, Jaipur
For free study notes log on :- www.gurukpo.com
Biochemistry-I
Published by :
Think Tanks
Biyani Group of Colleges
Concept & Copyright :
Biyani Shikshan Samiti

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ISBN: 978-93-81254-20-2
Edition : 2011
Price :
While every effort is taken to avoid errors or omissions in this Publication, any mistake or
omission that may have crept in is not intentional. It may be taken note of that neither the
publisher nor the author will be responsible for any damage or loss of any kind arising to
anyone in any manner on account of such errors and omissions.
Leaser Type Setted by :

Biyani College Printing Department
Preface
am glad to present this book, especially designed to serve the needs of the
students. The book has been written keeping in mind the general weakness in
understanding the fundamental concepts of the topics. The book is self-explanatory and
adopts the Teach Yourself style. It is based on question-answer pattern. The language
of book is quite easy and understandable based on scientific approach.
Any further improvement in the contents of the book by making corrections,
omission and inclusion is keen to be achieved based on suggestions from the readers
for which the author shall be obliged.
I acknowledge special thanks to Mr. Rajeev Biyani, Chairman & Dr. Sanjay Biyani,
Director (Acad.) Biyani Group of Colleges, who are the backbones and main concept
provider and also have been constant source of motivation throughout this Endeavour.
They played an active role in coordinating the various stages of this Endeavour and
spearheaded the publishing work.
I look forward to receiving valuable suggestions from professors of various
educational institutions, other faculty members and students for improvement of the
quality of the book. The reader may feel free to send in their comments and suggestions
to the under mentioned address.
Author
Biochemistry-I
Syllabus
B.Sc. Part-I
Biochemistry-I
Note : Question No. 1 shall consist of questions requiring short answers and shall cover entire
paper. The paper is divided to four sections. Students are required to attempt five questions in all
selecting not more than one question from each section. All questions carry equal marks.
Section-A
1. Concept of life and living processes : The identifying characteristics of a living
matter.
2. Cell membrane System and Cell wall : Cell Membrane and its Organization;
Elementary idea of cellular constituents : Nucleus, Mitochondria, Golgi bodies,
Endoplasmic reticulum, Lysosomes and Micrabodies; Bacterial and Plant Cell walls.
Section-B
1. Important properties of water, the law of mass action association of water and its
ionic product, pH, Bronsted acids, ionization of weak acids and Henderson Haeselbate
uation, Titration Curves, buffering action and physiologic offers.
2. Biomolecules : The small molecules of lifeSugars, Organ acids, amino acids and
nucleotides Macromolecules of life polysaccharides, fats, proteins and nucleic acids,
General idea of primary, secondary, tertiary and quaternary structure.
Section-C
1. Nucleus and Heredity: Nuclear mernbrane; Nucleolus, Nuclear pores; Chromosomes;
Packaging of DNA, DNA is Genetic material; DNA replication-basic concept : From
DNA to RNA: Ribosomes and protein synthesis.
2. Mitochondria and Release of Energy: Structure of organization and function;
Elementary account of Glycolysis and Krebs cycle and role of mitochondria in the later
process.
Section-D
1. Chloroplasts: Capturing energy from the sun: Structure organization and function;
Basic information on 'light' and 'dark' reactions of photopsynthesis and participation
chloroplast in the process in C3 + C4 and CAM plants.
2. Enzymes: Nomenclature and classification, co-enzymes and co-factors, reaction and

derivation of Michaelis-Menten equation kinetics and allosteric regulation of enzymes,
isozymes; more of catalysis.
3. Vitamins: Their structure, properties and Biological structures.
Biochemistry-I
Content
S. No.
1.
Name of Topic
Section-A
1. Concept of life & Living Processes
2. Cell Membrane System & Cell Wall
2.
Section-B
1. Important Properties of Water
2. Biomolecules
3.
Section-C
1. Nucleus & Heredity
2. Mitochondria & Release of Energy
4.
Section-D
1. Chloroplast : Capturing, Energy from Sun
2. Enzymes
3. Vitamins
5.
Unsolved Paper
Section-A
Chapter-1
Concept of Life & Living Processes

Q.1 Characteristics of living organisms include
A) the ability to adapt to the environment.
B) the ability to evolve over time.
C) possessing homeostatic mechanisms.
D) the ability to reproduce
E) All of the choices pertain to living organisms
Ans.: (E) All of the choices pertain to living organisms
Q.2 Which of the following sequences of organization is likely to be seen in a multicellular
organism, going from smallest to largest?
A) cell, organ, tissue, organism
B) cell, organ, system, tissue
C) cell, tissue, system, organism
D) organism, system, organ, tissue
E) tissue, system, cell, organ
Ans.: (C) cell, tissue, system, organism
Q.3 Which of the following characteristics is NOT required for the life of an individual
organism to continue?
A) to be organized
B) to respond
C) to metabolize
D) to reproduce
E) to acquire energy
Ans.: (D) to reproduce
Q.4
Which statement is FALSE about nearly all living things?

A) Living things are made up of cells.
B) Living things must obey the laws of chemistry and physics.
C) Living things show biological organization and other common characteristics of life.
D) Emergent properties can be used to distinguish living things from nonliving things.
E) Living things are composed only of organic elements, whereas nonliving things are
made up of inorganic elements.
Biochemistry-I
Ans.:
(E) Living things are composed only of organic elements, whereas nonliving things are
made up of inorganic elements.
Q.5 Which of these is the process by which changes occur in the characteristics of species of
organisms over time?
A) evolution
B) metabolism
C) adaptation
D) homeostasis
E) photosynthesis
Ans.: (A) evolution
Q.1
What are the identifying characteristics of Living matter?
Ans.: (i)
Living organisms are highly complicated and organized structures and

contain large number of different organic molecules.
(ii)
Each component unit of a living object appears to have specific purpose or

function.
(iii)
The living organism have ability to extract, transform and use energy from
their environment either in form of organic nutrients or radiant energy of
sunlight.
(iv)
The most remarkable attribute of living organism is their capacity for self
replication.
Q.2
Write axioms or principles of Living State.
Ans.: (i)
There is basic simplicity in structure of biological molecules.
(ii)
Living organisms use same kind of building block molecules and appear to
have common ancestry.
(iii)
Identities of each species or organism are preserved by its possession of

distinctive sets of nucleic acid and proteins.
(iv)
All biomolecules have specific functions in cells.
(v)
Living organisms create and maintain their complex, orderly, purposeful

structures at the expense of free energy.
(vi)
Living cells are self-regulating chemical engines.

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(vii)
It maintains itself in dynamic steady state far from equilibrium with its
surrounding.
(viii) Genetic information is encoded in units that are submolecular in

dimensions.
(ix)
It carries out various reactions catalyzed by biocatalyst or enzymes.
(x)
The energy needed is provided directly or indirectly by solar energy.
Biochemistry-I
11
Chapter-2
Cell Membrane System & Cell Wall

Q.1 Cell organelles are embedded in
A) Nucleolus
B) Cytoplasm
C) Protoplasm
D) Mitochondria
Ans.: B) Cytoplasm
Q.2 Which of the following correctly matches an organelle with its function?
A. mitochondrion . . . photosynthesis
B. B)nucleus . . . cellular respiration
C. ribosome . . . manufacture of lipids
D. lysosome . . . movement
E. central vacuole . . . storage
Ans. (e) central vacuole . . . storage
Q.3 Which one of the following is not a constituent of cell membrane?
A. Phospholipid
B. Glycolipids
C. Cholesterol
D. Proline
Ans.: (D) Proline
Q.4 Plasma membrane is made up of
A. Protein, Lipids, Carbohydrates
B. Protein, lipids
C. Protein
D. Protein, Cabohydrates
Ans.: A) Protein, Lipids, Carbohydrates
Q.5 Which of the following are all present in animal cells
A. mitochondria, cell membrane, cell wall, cytoplasm
B. chloroplasts, cytoplasm, vacuole, nucleus
C. nucleus, cell membrane, mitochondria, cytoplasm
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D. vacuole, cell membrane, nucleus, mitochondria

Ans.: (C) nucleus, cell membrane, mitochondria, cytoplasm
Q.6 What cell organelle is responsible for the production of ATP?
A. chloroplast
B. nucleus
C. vesicle
D. Mitochondrion
Ans.: (D) Mitochondrion
Q.7 Which increases the fluidity of the plasma membrane?
a) having a large number of membrane proteins
b) the tight alignment of phospholipids
c) cholesterol present in the membrane
d) double bonds between carbon atoms in the fatty acid tails.
Answer: (d) double bonds between carbon atoms in the fatty acid tails.
Q.8 Which best describes the structure of a plasma membrane?
a) proteins embedded within two layers of phospholipids
b) phospholipids sandwiched between two layers of proteins
c) proteins sandwiched between two layers of phospholipids
d) a layer of proteins on top of a layer of phospholipids
Answer: (a) proteins embedded within two layers of phospholipids
Q.9 The function of rough endoplasmic reticulum is to synthesize
a- lipid
b- carbohydrate
c- protein that will be secreted by the cell
d- cytoplasmic protein necessary of the cell own existence
e- glycogen
Ans.: c- protein that will be secreted by the cell
Q.10 Organelles involved in the process of secretion
a- endoplasmic reticulum (rough & smooth)
b- Golgi body
c- Cell membrane
d- cytoskeleton
Ans.: Both (a) and (b)
Q.11 Hydrolytic enzymes are found in
a- Golgi apparatus
b- RER
c- SER
d- Lysosomes
e- Ribsosomes
Ans.: (d) Lysosomes
Q.12 Ribosomes
a- are attached to the surface of the nuclear membrane
Biochemistry-I
13
b- are organized into polysomes in cells synthesizing intracellular proteins

c- are always associated with a strand of mRNA
d- are surrounded by a delicate thin membrane
Ans.: b- are organized into polysomes in cells synthesizing intracellular proteins
Q. 13 The nucleus is
a- always found one per cell
b- an essential organelle present in all complete cells
c- enclosed within a nuclear membrane
d- enclosed within inner, intermediate, and outer unit membrane
e- completely covered externally by the fibrous lamina
Ans.: Both B and C
Q.14 Which of the following organelles is not self-replicating?
a. Mitochondria
b. Peroxisomes
c. Proteasomes
d. Chloroplasts
Ans.: Proteasomes
Q.15 Double membrane is absent in (a)Mitochondrion (b) Chloroplast (c) Nucleus (d) Lysosome
Ans.: (d) Lysosome
Q.1
Give brief account on Membrane Phospholipids?
Ans.: Plasma membrane is a dynamic, fluid structure and forms the external boundary
of cells. It acts as a selectively permeable membrane & regulated the molecular
traffic across the boundary. Basic Structure of plasma membrane is phospholipids
bilayer. The plasma membrane of animal cells contain four major phospholipids
such as; phosphatidyl choline, phosphatidyl serine, phosphatidyl ethanolamine,
sphingomyelin.
Phospholipids are amphipathic molecules and have a hydrophobic portion &
hydrophilic portion. The primary physical forces for organizing biological
membranes are hydrophobic interactions between the fatty acid chains of lipid
molecules. These interactions result in formation of a phospholipid bilayer sheet
containing two layers of phospholipid molecules whose polar head groups face
surrounding watery surface while fatty acid chain form continous hydrophobic
interior.
14
In addition to phospholipids plasma membrane of animal cells contains

glycolipids and sterol. Glycolipids contain sugar residue covalently attached to
lipid. Cholesterols is especially abundant in plasma membrane of animal cells,
plants prokaryotes lack the same. Fluidity of bilayer depends on its lipid
composition, cholesterol content and temperature.
Q.2
Write short note on Membrane Proteins?
Ans.: Many proteins are associated with membrane they can be grouped as peripheral
proteins
and integral membrane proteins.
(a)
Peripheral proteins: Also called as extrinsic proteins; they do not interact

with phospholipid bilayers hydrophobic core, instead they are usually
bond to membrane indirectly by interactions with integral membrane
proteins or directly by interactions with lipid polar head groups e.g.
spectrin and ankyrin present in membrane of RBC.
(b)
Integral membrane proteins: Proteins that held in bilayer by unusually

tight binding to other proteins or lipids & can not be released easily are
called integral membrane proteins also known as intrinsic proteins. They
have one or more segments embedded in phospholipids bilayer & contain
residues with hydrophobic side chains that interact with fatty acyl groups
of membrane phospholipids & thus anchoring protein to membrane.
Proteins associated with membrane can be released from membrane by
gentle extraction procedures such as exposure to high or low ionic strength
solution or of extreme pH.
Following are the various Types of Integral Membrane Proteins:

(a)
Transmembrane Proteins: Most integral proteins span entire

phospholipids bilayer. They can be multi pass or single pass. Examples
glycophorin and band 3 proteins present in plasma membrane of RBC.
(b)
Lipid Anchored Protein: Some proteins are anchored to membrane by

covalent bonds. In these proteins bound fatty acid is embedded in
membrane, but polypeptide is chain doesnt enter into bilayer.
Biochemistry-I
Q .3
15
Write in detail about Mitochondria?
Ans.: Mitochondria were first observed by Kolliker as globular structure in striated

muscles. The present name Mitochondria was given by Benda. Mitochondria
move autonomously in cytoplasm, so they generally have uniform distribution in
cytoplasm.
Mitochondria have definite orientation for example, in cylindrical cells; the
mitochondria usually remain oriented in basal apical direction and lie parallel to
main axis. The number of mitochondria in a cell depends on type and functional
state of cell. It varies from cell to cell & from species to species in shape
Mitochondria may be filamentous or granular in shape and may change form one
shape to another. Normally mitochondria vary in size from 0.5 m to 2.0 m.
Structure: Each mitochondrion is bounded by two highly specialized membranes
that play crucial part in its activities. Each of mitochondrial membrane is 6 nm in
thickness and fluid mosaic in ultra structure. The outer membrane is quite
smooth and has many copies of transport protein called porins which form large
aqueous channels through the lipid bilayer. Inside and separated from outer
membrane is present the inner membrane. The inner membrane is not smooth but
is impermeable and highly convoluted forming series of infolding called cristae in
matrix space. Mitochondria have double membrane envelops in which inner
membrane divides the mitochondrial space into distinct chambers :
(i)
Outer Compartment
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(ii)
Peri-mitochondrial Space
(iii)
Inner Compartment or Matrix Space
Inner chamber or Matrix space is filled with dense, homogenous, gel like
proteinaceous material called mitochondrial matrix. Inner membrane has an
outer cytosol or C-face toward peri mitochondrial space & an inner matrix or m
face toward matrix. Attached to M face of inner mitochondrial membrane are
repeated units of stalked particles, called Elementary particles, inner membrane
subunit oxysomes. They are also identified as F1 particles are meant for ATP
synthesis.
Mitochondrial Isolation: Following are the three types of methods for
Mitochondrial Isolation:
(i)
Direct Observation of Mitochondria: Direct examination with vital stain

called Janus Green which stains living mitochondria greenish blue due to
its cytochrome oxidase activity.
(ii)
Cell Fractionation: Mitochondria can easily be isolated by differential

centrifugation at 20,000 to 40,000 g.
(iii)
Cytochemical marking: Different parts of Mitochondria have distinct

marker enzyme for histochemical marking such as cytochrome oxidase for
inner membrane, malate dehydrogenases for matrix and adenylate kinase
for outer chamber.
Enzymes present in Mitochondria:

Biochemistry-I
17
(i)
Enzymes on outer Membrane: Monoamine oxidase, cytochrome reductase,

fatty acid CoA ligase & enzyme involved in lipid synthesis.
(ii)
Enzymes on Inner Membrane: ATP synthetase that makes ATP in inner

membrane, specific transport proteins Succinate dehydorgenase four
cytochromes cyt b, cyt c, cyt c1, cyt a and cyt a3.
(iii)
Enzymes on Inter membrane space: Enzymes require to phosphorylate the

other nucleotides enzymes like adenylate kinase, nucleoside
diphospokinase .
(iv)
Enzymes on Mitochondrial Matrix: Enzymes that required for oxidation of

pyruvate and fatty acids and for citric acid cycle or kreb cycle.
Matrix contain: Malate dehydrogenase, Isocitrate dehydorgenase,

fumarase, aconitase, citrate synthetase, -keto acid dehydrogenase.
Q.4
Describe structure and function of Golgi apparatus?
Ans.: Golgi apparatus was discovered by Camilo Golgi in 1873. It occurs in all cells
except the prokaryotic cells and eukaryotic cells of certain fungi, pteridophytes.
Their number per cell vary several hundred in different organisms. In animal cell
they usually occurs as a single golgi apparatus,but its number may vary from
animal to animal from cell to cell.
In the cell of higher plants the golgi bodies or dictyosomes are usually found
scattered throughout the cytoplasm. The golgi apparatus is morphologically very
similar in both plants and animal cells, the detailed structure of three basic
components of the golgi apparatus are:
(i)
Flattened Sac or Cisternae : are central, flattened plate like or saucer like
closed compartments which are held in parallel bundles or stacks one
above the other. Each cisternae forms dictyosome which may contain 5 to 6
golgi cisternae in animal cells. Each cisternae is bound by smooth unit
membrane.
(ii)
Tubules: Complex array of associated vesicles and anastomosing tubules.
(iii)
Vesicles : are of three types(a) Transitional vesicle: Small & form as blebs from Endoplasmic vesicle
and converge to golgi.
(b) Secretory vesicles: are of varied size, discharge of from margins of
cisternae of golgi.
Clathrin Coated vesicles: Spherical protuberance found at periphery of the

organelle usually at ends of single tubules & distinct from secretary vesicles.
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The GERL region: Golgi apparatus is spatially and temporally related to

endoplasmic reticulum and also found in origin of primary lysosomes. GERL is
region of sorting of cellular secretary protein.
Functions: Golgi vesicles are often referred to as the traffic police of cell. This play
a key role in sorting many of cell proteins & membrane constituents and in
directing them to proper destination.
Recently in functions of golgi apparatus sub compartmentalization with a
division of labour has been proposed between cis & trans golgi in which most
refined proteins are further separated for their delivery to various cell
compartments. Golgi apparatus is a centre for reception, finishing, packaging and
dispatch for a variety of materials in animal & plants cells.
In plants Golgi apparatus is mainly involved in secretion of materials of primary
and secondary cells wall. During cytokinesis of mitosis or meiosis, the vesicles,
originating from periphery of Golgi apparatus coalesae in the phragmoplast area
to form semi solid layer called cell plate. The unit membrane of golgi vesicles
fuses during cell plate formation and becomes part of plasma membrane of
daughter cells.
In animals golgi appartus is involved in packaging and exocytose of following
materials :
Q.5
(i)
Zymogen of exocrine pancreatics cells
(ii)
Mucus secretion & goblet cells of intestine.
(iii)
Also involved in formation of certain cellular organelles such as plasma

membrane, lysosomes, acrosome, and cortical granules of variety of
oocytes.
Describe structure and function of Endoplasmic Reticulum?
Ans.: The name endoplasmic reticulum has been coined by Porter. The occurrence of
endoplasmic reticulum vary from cell to cell. The cells of those organs which are
actively engaged in the synthesis of proteins such as acinar cell of pancreas,
plasma cell of some endocrine glands are found to contain rough endoplasmic
reticulum (RER is endoplasmic reticulum with ribosomes).
ER & Endomembrane System: ER is also called as cytoplasmic vacuolar system is
main component of endomembrane. This system along with nuclear membrane
Biochemistry-I
19
and golgi apparatus form endomembrane system.. GERL refers to as special

region of endmembrane system.
Morphology : ER occurs in following three forms :
(i)
Lamellar form or cisternae
(ii)
Vesicular form or Vesicles
(iii)
Tubular Form or tubules
Cisternae: are long flattened sacs like rough endoplasmic reticulum exsist as
cisternae which occur in those cells which have synthetic roles as the cells of
pancreas, notochord and brain.
Vesicles: are oval, membrane bound vascular structure having, often remain
isolated in cytoplasm & occur in most cells but abundant in smooth endoplasmic
reticiulum.
Tubules: Branched structures forming reticular system along with cisternae and
vesicles. Often found in SER & associated with membrane movements.
Types:
(a)
Agranular/SER: Smooth walls because the ribosomes are not attached with
its membranes. It is generally found in adipose cells, interstitial cell.
Muscles are also rich in smooth endoplasmic reticulum.
(b)
Granular / RER : Possess rough wall because ribosomes remain attached

with its membrane. It is found abudantly in those cells which are active in
protein synthesis such as pancreatic cells, plasma cells etc. In RER,
ribosomes are often present as polysomes held together on mRNA and are
arranged in rosetts or spirals.
Origin of Endoplasmic Reticulum: It is normally assumed that the ER has

originated by evagination of nuclear membranes. The synthesis of membranes of
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ER is found to proceeto in following direction RER SER. In fact membrane

biogenesis is a multi step, process involving, first synthesis of basic membrane of
lipids and intrinsic proteins, thereafter addition of other constituents like sugars,
lipids etc.. The process by which a membrane is modified is called membrane
differentiation.
Functions of Endoplasmic Reticulum:
(A)
(B)
(C)
Common Functions of Granular & Agrangular :

(i)
ER provides mechanical support & skeletal framework to all
(ii)
Exchange of molecules by process of osmosis, diffusion and active

transport occurs through ER membranes
(iii)
Contain many enzymes which perform various synthetic and

metabolic activities.
(iv)
It acts as an intracellular circulating or transporting system.
(v)
It can form the new nuclear envelop after each nuclear decision
(vi)
It plays important role in releasing column which muscle is

stimulated and activity transporting colleen back into ER.
Function of Smooth ER:

(i)
Synthesis of lipids
(ii)
Sterol Metabolism
(iii)
Detoxification
(iv)
Glycogenolysis and blood glucose homeostasis.
(v)
Synthesis of triglycerides and of vesicle pigments.
Functions of Rough ER:

(i)
Synthesis of Protein
(ii)
Protein glycosylation
(iii)
The proteins for secretion, lysosomes and membrane formation are

synthesized on membrane bound ribosome.
Enzymes on ER Membranes
S.No.
Enzyme
Surface localization
Cytocrome b5
Cytoplasmic face
NADP-cytochromic C reductase
-do-
Biochemistry-I
Q.6
21
ATPase
-do-
- glucouronidase
Luminal face
Cytochrome P-450
Cytoplasmic & Luminal

face
GDP-Mannosyl transferase
Cytoplasmic face
Write detail account on Microbodies?
Ans.: Microbodies are organelle having central granular or crystalloid core containing
some enzymes.
Structure and Types : Microbodies are spherical or oblate form bounded by
single membrane and have interior or matrix which is amorphous granular.
Recent biochemical studies show distinguished two types of Micorbodies namely,
peroxisomes & glyoxysomes.
Peroxysomes: Occur in animal cells and in wide range of plants. Peroxysomes are
variable in size & shape they have single unit membrane of lipid and protein
molecules which encloses granular matrix.
Function:
(i)
Peroxysomes are so called because they usually contain one or more

enzymes that use molecular oxygen to remove hydrogen atoms from
specific organic substrate.
RH2 + O2 R + H2O2
H2O2 + RH2 R + 2H2O
of detoxify reactions. The enzymes catalase is present in peroxysomes.
When excess H2O2 accumulates in cell, catalase converts H2O2 to H2O.
(ii)
Peroxysomes of plant leaves contain catalase together with enzymes of

glycolate pathway as glycolate oxidase, gratamate glyoxylate sereire
glyoxylate and aspartate & keto glutarate the slycolate cycle thought about
to bring formation of aneeu a cids like glycene, serine.
(iii)
In green leaves there are peroxysomes that carry out procose called
photorespiration in which glocation and is released from chloroplast and
owxidized into glyoxfate & H2O2 by peroxisomal enzyme called fycolic
acid oxidase.
22
(iv)
Peroxisomes of rat liver cell contain enzymes of -oxidation for

metabolism of fatty acids, the acetyl CoA formed by this process is
transported to mitochondrial where it enters to citric acid cycle.
(v)
Mammalian cells do not contain D-amino acid but peroxisomes of

mammalian liver & kidney contain D-amino acid oxidase. Its possible role
is to initiate degradation of D-amino acid that may arise from break down
of peptidoglycan
(vi)
Glyoxysomes: Found to occur in cells of yeast neurosporo and higher

plants. They resemble peroxisomes in morphological details. There
crystalloid core consists of dense rods of 6.0 um diameter. They have
enzymes for fatty acid metabolism and glycogenesis. Glyoxysomes
perform following biochemical activities of plant cells.
(i)
During germination of oily seeds, the stored lipid molecules of

spherosomes are hydorlysed by enzyme lipase to glycerol & fatty acids.
During -oxidation process, the fatty acid breakdown to molecules of
acetyl COA molecules. In plant oxidation occurs in seeds. In plant cells
the acetyl COA, product of -oxidation, chain is not oxidized by Kreb cycle
because it remain spatially separated from the enzymes of Kreb cycle
instead, acetyl CoA undergoes glyoxylate cycle to be converted into
succinate.
(ii)
Glyoxylate cycle occurs in glyoxysomes and it invokes some of the

reactions of Kreb cycle. The citrate formed converted to isocitrate &
isocitrate to glyoxylate and succinate.
Isocitrate
Glyoxylate + Succinate
AcetylCoA + Glyoxylate
2 AcetylCoA + NAD+
Malate
Malate dehydrogenase
Succinate + NADH+H +
Succinate is end product of glyoxysomes metabolism of fatty acid and is

not further metabolized in this organelle.
Q.7
What are Lysosomes?
Ans.: Lysosomes were initially described as perinuclear dense bodies by C. de Duve

renamed these organelles as Lysosomes to indicate the internal digestive enzymes
only become apparent than the membrane of these organelles as lysed.
Lysosomes occur in most animal and plant cells, absent in mature mammalian
RBC. They occur in abundance in epithelial cell of lungs and uterus. Phagocytic
cells and cells of reticulo endothelial system are also rich in lysosomes.
Biochemistry-I
23
Structure: Lysosomes are round vacuolar structures which remain filled with
dense material bounded by single unit membrane.
It should contain two or mores acid hydordases and should demonstrate the
property of enzyme.,when treated in a way that adversary effects organelles
membrane structure.
Lysomal enzymes: Lysosomes contain 40 types of hydrolytic enzymes, they
include proteases, nucleases, glycosidases, lipases, phospholipases, phosphatases
sulphatases. All lysosomal enzymes are acid hydrolases. Acid dependency of
lysosomal enzymes protects the contents of cytosol against any damage if leakage
of lysosomal enzymes should occur.
Function of Lysosomes :
(i)
Digestion of Large extra cellular particles which enables to devour the
foreign bacteria of verieses
(ii)
Digestion of intracellular substances like protein, lipids and carbohydrates
of the cytoplasm & supply to cell, necessary amount of energy.
(iii) Autolysis or Cellular Autophagy : In pathological conditions the
lysosomes start to digest the various organelles. When cell dies, the
lysosmal membrane ruptures and enzymes are liberated. These enzymes
digest dead cell.
(iv) Extra Cellular Digestion: The lysosomes of certain cells such as sperms
discharge their enzymes outside the cell during the process of fertilization,
the lysosomal enzyme digest the limiting membrane of ovum and forms
penetration ratio. Acid hydrolases are also released from osteoclast &
break down bone for the reabsorbtion.
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Lysosome and Disease: Malfunctioning of lysosome often results in various

pathological disorders eg; Tay Sachs disease which is inborn disorder, other
induced by environmental pollution eg; s silicosis.
Lysosomes in Plants : Plant contain several hydrolases. Plant lysosomes can be
defined as membrane bound cell compartment containing hydrolytic digestive
enzyme. vacuoles in plants have been divides in following types:
(a)
Vacuoles: formed by fusion of to small provacuoles which are believed to
be derived from ER and Golgi and contain acid hydrolases. Enzymes are
associated with tonoplast of large Vacuole of differentiating cells.
(b)
Spherosomes : Membrane bound spherical particles occurring in most
plant cells they have fine granular structure rich in lipids and proteins.
They originate from ER, like lysosomes they are not only responsible for
the accumulation and mobilization of reserve lipids but also for the
digestion of other cytoplasmic components in corporated by phagocytosis.
(c)
Aleurone Grains: The aleurone Grains or protein bodies are spherical
membrane bound storage particles occurring in cells of endosperm and
cotyledons of seed they are formed during later stages of seed ripening
and disappear in early stages of germination. Thus like spherosome,
aleurone store reserve materials, mobilize them during germination and in
addition form comportment for digestion of other cell components.
Q.8
Describe structure and function of Nucleus.
Ans.: Nuclei were first discovered and named by Robert Brown and were quickly
recognized as constant feature of all animal and plant cells. Nucleoli was first
noticed by Fontana , Strasburger introduced the term cytoplasm and
nucleoplasm.
Nucleus is found in all eukaryotic cells of plants and animals. However
mammalian erythrocyte contains no nucleus. The prokaryotic cells of bacteria do
not have true nucleus i.e single circular and large DNA molecules remains in
direct contact with cytoplasm. Usually nucleus remains located in the centre. But
its positions may change time to time according to metabolic status e.g., in
embryonic cells nucleus generally occupies geometric centre of cells but as the cell
start to differentiate, displacement in nucleus position will take place.
Morphology: Usually cells contain single nucleus but the number of nucleus may
vary from cell to cells, most plant and animal cells are uninucleate. The shapes of
nucleus remain related to shape of cell. The nuclei of cylindrical, prismatic or
fusiform cell contain ellipsoid nucleus whereas, cells of squamous epithelium
contain discoidal nuclei.
Ultra-structure:
Biochemistry-I
25
(i)
Nuclear Envelope: Nuclear envelope encloses DNA and defines the

nuclear compartment of inter phase and prophase nuclei. It is formed of
true concentric unit membranes, the spherical inner nuclear membrane
contain specific proteins that act as binding site for supporting fibrous
sheath of inter mediate filaments called nuclear lamina. The inner nuclear
membrane is surrounded by the outer nuclear membrane which closely
resembles the membrane of endoplasmic reticulum, outer surface of outer
membrane has ribosomes engaged in protein synthesis The space between
inner and outer membrane is called peri nuclear space. The perinuclear
space is fluid filled compartment which is continuous with ER lumen.
(ii)
Nuclear Lamina: Also called fibrous lamine It is a protein meshwork and

present inside surface of inner nuclear membrane, except the areaof
nucleopores and consist of intermediate filaments also it is very dynamic
structure. In mammalian cells undergoing mitosis, the transient
phosphorylations of several serine residues on lamins causes the lamina to
dissamble.
(iii)
Nuclear Pore Complex: The nuclear envelop in all eukaryotic forms is

perforated by nuclear pores, nuclear pore appear circular in surface view
and diameter between 10 nm -100 nm. Nuclear pore complex consists of
two rings at it periphery and large particle that forms a central and radial
spokes ,partices anchored to cytoplasmic ring are thought to bind
ribosomes. The hole in the centre of pore complex is aqueous channel
through which water soluble molecules shuttle between nucleus and
cytoplasm. In nuclei of mammals it has been calculated that nuclear pores
account for 5-15% of surface area of the nuclear membrane. The number of
pores in nuclear envelop or pore density correlate with activity of cell.
Nuclear pore are evenly distributed in somatic cells, however in other cell
pores are arranged in rows or clusters.
(iv)
Nucleoplasm : Space between nuclear envelop and nucleus is filled with

ground substance or matrix called nuclear sap or nucleoplasm.
26
Q.9
Describe Plant & Bacterial Cell Wall.
Ans.: The plant cells is always surrounded by cell wall which is a nonliving structure
formed by living protoplast. It is rigid and protective layer around the plasma
membrane which provides mechanical support to the cell. It also determines the
shape of plant cell.
Cellulose : The polysaccharide of cell wall include polymer of glucose unit linked
by 1-4 glycosidic bonds. Its structural units known as micro fibrils which get
associated with macrofibrils. Hemicullose are short but branched heteropolymers
of various monosaccharides. Some of common eg: of hemicellulose are xylans,
glucomannans
Pectins : Water soluble, heterogenous branched polysaccharide that contain many
negatively charged D- galatouronic acid residues along will D-glucuronic acid
residues ,they are helpful in keeping cell wall component together. Mannans,
agar, lignin and chitin are also present in cell wall.
Biochemistry-I
27
Cutin : Is a biological plastic and is made of fatty acid. Suberin is water resistant
substance, comprising of fatty acid and found in Cork and Cell wall of many
plants.
Structure:
(i)
Primary Cell Wall: First formed cell wall, outer most layer of cell and
comparatively thin, the primary cell wall of yeast and fungi is composed of
chitin.
(ii)
Secondary Cell Wall: Primary cell wall is followed by secondary cell wall.
It is thick permeable and composed of compactly arranged macrofibrils of
cellulose.
(iii) Tertiary Cell Wall: There occurs another cell wall beneath the secondary
cell wall called as tertiary cell wall. Tertiary differs in staining, chemical
composition, besides cellulose, tertiary wall also consist of xylem.
Middle Lamella: Cell of plant tissues generally remain cemented together by an
inter cellular matrix known as middle Lamella. It is mainly composed of pectin
and lignin. Each plant cell is interconnected with each other through cytoplasmic
channels called Plasmodesmata which pass through intervening cell wall.
Origin and Growth of Cell Wall: It includes formation of matrix and synthesis
and orientation of cellulose microfibrils. Extension of cellulose microfibril is
presumably achieved by lateral movement of enzyme complex in fluid phase of
plasma-membrane. During lignifications, lignin is deposited in spaces between
the cellulose molecules making cell wall more rigid rendering it impermeable.
The lignified tissue becomes well adapted to two types of functions:
(i)
It provides mechanical strength due to it lingo- cellulose composition
(ii)
It transports water & salts, since lignifications involve loss of the

protoplasm resulting in formation of hollow waterproof tube.
Bacterial Cell Wall: Present outside plasma membrane in all the bacteria. It is
very thick in gram positive bacteria and is comparatively thin in gram negative
bacteria. The cell wall in bacteria is much more complex then cellulose wall of
plant cells. It is formed of mucopeptide, polysaccharide, amino acid and lipid.
Polysaccharides: Forms backbone of cell wall and confer structural rigidity, the
polysaccharide of bacterial wall formed of sugars like glucose, galactose.
(i)
N-Acetyl Muramicic Acid
(ii)
N-Acetyl Glucosamine
28
They are arranged alternatively and joined by glycosidic linkages. In gram

positive bacteria matrix of cell wall formed of teichoic acid which is polymers of
glucose, alanine and glycerol or Ribitol. Techoic acid has glycerol or ribitol
phosphate and only one of the two can be present in cell wall of particular strain
of gram positive bacteria.
In gram negative bacteria there is no teichoic acids and only 5-10%
peptidoglycans present which protect cell from osmotic rupture and provide
rigidity and shape to cell wall. Teichoic acids if present obtain Mg+2 from
environment for metabolic function of cell.
Amino acid: Amino acid present are glutamic acid, alanine, glycine, and lysine. In
gram positive bacteria amino acids are alanine & glycine which are present in
large proportions.
Lipids: About 20% lipid present in cell wall of gram negative bacteria and in
gram positive bacteria only traces of lipid found.
S.No.
Gram Positive Bacteria
Gram Negative Bacteria
1.
Cell Wall is thick.
It is thin.
2.
95% Peptidoglycans.
Peptidoglycans are 5-10%of

cell wall.
3.
Teichoic acid present.
4.
Lack LPS- lipopolysaccharides
Absent.
Cell wall contains LPS which
make them virulent
5.
Four types of amino acids are Many types of amino acids are
present in major proportion present.
thats mainly include glycine,
alanine
Difference between gram positive & gram Negative bacterial cell wall.
Biochemistry-I
29
Section-B
Chapter-1
Important Properties of Water

Q.1 In a single molecule of water, two hydrogen atoms are bonded to a single oxygen atom
by
A) hydrogen bonds.
B) nonpolar covalent bonds.
C) polar covalent bonds.
D) ionic bonds.
E) van der Waals interactions.
Ans.: B) nonpolar covalent bonds.
Q.2 An example of a hydrogen bond is the bond between
A) C and H in methane (CH4).
B) The H of one water molecule and the O of another water molecule.
C) Na+and Cl- in salt.
D) the two hydrogen atoms in a molecule of hydrogen gas (H2).
E) Mg+and Cl- in MgCl2.
Ans.: B) the H of one water molecule and the O of another water molecule.
Q.3 Water is able to form hydrogen bonds because
A) oxygen has a valence of 2.
B) the water molecule is shaped like a tetrahedron.
C) the bonds that hold together the atoms in a water molecule are polar covalent bonds.
D) the oxygen atom in a water molecule has a weak positive charge.
E) each of the hydrogen atoms in a water molecule is weakly negative in charge.
Ans.: C) the bonds that hold together the atoms in a water molecule are polar covalent
bonds.
Q.4 What gives rise to the cohesiveness of water molecules?
A) hydrophobic interactions
B) nonpolar covalent bonds
C) ionic bonds
D) hydrogen bonds
E) both A and C
Ans.: D) hydrogen bonds
Q.5 Water molecule has characteristics of
(A) Acid
(B) Base
30
(C) Both acid and base

(D) None of these
Ans.: C) Both Acid and Base
Q.6 A substance that prevents large changes in the pH of a solution is
A. DNA.
B. water.
C. a buffer.
D. an enzyme.
Ans.: C. a buffer.
Q.7 If the pH of a solution changes from 2 to 5, then the solution has
A. become a base.
B. lost hydrogen ions.
C. become more acidic.
D. gained hydrogen ions.
Ans.: B. lost hydrogen ions.
Q.8 Water allows chemical reactions in cells to occur because it
A. acts as a solvent.
B. evaporates readily.
C. is less dense as a solid.
D. promotes dehydration synthesis
Ans.: A. acts as a solvent.
Q.9 Water molecules are connected to each other by
A. buffers.
B. hydrolysis.
C. peptide bonds.
D. hydrogen bonds.
Ans.: D. hydrogen bonds.
Q.10 Which of the following is necessary for hydrogen bonding?
A. Peptide bonds.
B. Hydrogen ions.
C. Polar molecules.
D. Equal sharing of electrons.
Ans. C. Polar molecules.
Q. 1
Define Buffer?
Ans.: A Buffer solution is one that resists a change in pH after addition of acid (H+) or
base (OH-) more effectively than an equal volume of water.
Q.2
What are the unique features of Water?

Biochemistry-I
31
Ans.: Following are the unique features of water:
Q.3
(1)
Water is universal solvent.
(2)
It adheres and cohesive.
(3)
Resists changes in temperature
(4)
Resists change of state.
Summarize the physical properties of Water?
Ans.: Physical Properties of water are:

Property
Q.4
Melting Point :
0C
Boiling Point :
100C
Heat of Vaporization :
540 cal/g
Heat Capacity :
1000 cal/g
Heat of Fusion :
79.7 cal/g
Surface Tension :
72.8
Dielectric Constant :
80
What are the properties of Water of physiological importance?
Ans.: (1)
Q.5
Value
Expansion on freezing and frozen water is less dense than liquid water.
(2)
High surface tension because of which water rises in narrow capillary tube.
(3)
High heat capacity and thus water act as temperature buffer.
(4)
High solvent power and therefore it is called universal solvent which

facilitates chemical reactions both outside and within biological systems.
State Law of Mass Action? What is ionic product of Water?
Ans.: Low of Mass Action states, The rate of a chemical reactions is directly
proportional to product of molar concentrations reactants at a constant
temperature at a given time.
e.g. A + B
Products
Thus, Rate of reaction r
[A] [B]
32
=k [A] [B] where [A] and [B] are molar concentrations of reactants A & B
respectively. k is constant of proportionality called rate constant.
For, reversible reaction A + B ---- X + Y
Keq =
[X][Y]
[A][B]
Keq = equilibrium constant
Water molecule have slight tendency to under go reversible ionization crucial to

role of water in cellular functions.
H2 O
H+ +OH
From Law of Mass action; the equilibrium constant for reversible ionization of
water can be given by
Keq =
[H ][OH ]
[H2O]
_ _ _ (1)
In pure water at 25C concentration of water is 55.5 M. On substituting 55.5 M in

equilibrium constant expression.
[H + ][OH - ]
Keq =
55.5M
or (55.5 M) (Keq) = [H + ][OH - ] = Kw
_ _ _ (2)
_ _ _ (3)
Kw = (Keq) (55.5 M) is called as:

Ionic Product of water
Value for Keq = 1.8 x 10-16M at 25 C
(55.5) (1.8 x 10-16) = [H + ][OH - ]
Or 1.0 x 10-14M2 = [H + ][OH - ] = Kw
If in solution there is equal concentration of H+ & OH- then,
Kw = [H+] [H+]
as, [OH] = [H+]
Kw = [H+]2
Or
Q.6
Kw = H+ = 110-14 M2 = 10-7 M
Define pH. Why it is required to maintain pH?
Ans.: Sorensen defines pH of a solution as the negative logarithm of concentration of

hydrogen ions.
Biochemistry-I
Thus,
33
pH = log
1
= -log [H + ]
+
[H ]
The symbol p denotes negative logarithm of .

For, precisely natural solution at 25 C, in which concentration of hydrogen ion is
1.0 x 10-7 M pH can be calculated as:
pH
1
= - log (1 107 )
7
1 10
log 1.0 + log 107
0 + 7.0
Log
=
=
=
7.0
Measurement of pH is one of the most important and frequently used procedures
in biochemistry. It is required to maintain pH because it affects structure and
activity of biological macro molecules for e.g. catalytic activity of enzymes.
Q.7
Write about Brownsted Acids?
Ans.: In aqueous systems addition or removal of hydrogen ion is explained by

Brownsted-Lowry concept of acids and bases.
A Brownsted Lowry acid is defined as substance that can donates a proton (H+)
and Brownsted Lowry base is substance that can accept a proton. A proton donor
(acid) and corresponding proton acceptor (base) make up conjugate acid base
pair.
HA H+ + A
Here, HA represent Brownsted Lowry acid.
Q.8
Write in brief on Ionizations of weak Acid?
Ans.: Weak acid is molecule that has a lesser tendency to lose its proton and therefore
does not readily dissipate in water for e.g. Acetic acid (CH3 COOH).
The dissociation of weak organic compound, acetic acid is written as:
CH3COOH H+ + CH3COO
At a given temperature, extent of ionization at equilibrium can be given by
following equation.
Ka =
[H+ ][CH3COO ]
[CH3COOH]
Ka- apparent ionization constant.

For 1M acetic acid, Ka = 1.8 x 10-5 M at 25 C if [H+] & [CH3 COO-] = x
34
x2 = 1.8 x 10-5
x = 4.2 x 10-3 M
= 0.0042 M
Q.9
What is Henderson Haessel Bach Equation?
Ans.: The quantitative relationship among pH, buffering action of mixture of weak acid
with its conjugate base, and the pka of weak acid is given by a simple expression
called Henderson Haesselbach equation. The shape of titration curves of weak
acid is also expressed by this equation .It is simply a useful way of restating
expression for dissociation constant of a weak acid. For dissociation of a weak
acid HA into H+ and A-, the Henderson Haesselbach equation can be derived as;
Ka =
Or
[H + ][A ]
[HA]
[H+] = Ka
[HA]
[A ]
Taking log
log [H+] = log Ka + log
[HA]
[A ]
taking negative log both side;

- log [H+] = - log Ka [ log
[HA]
]
[A ]
Substitute pH for log [H+] and pKa for log Ka

pH = pKa [log
Or
[HA]
]
[A ]
[A ]
pH = pKa + log
[HA]
In more general form;

pH = pKa + log [Proton acceptor]
[Proton donor]
This equation fits titration curve of all weak acids and enables to deduce a
number of important quantitative relationships.
Biochemistry-I
35
Q.10 Explain Buffering Action of following Biological or Physiological Buffers.

OR
Write a short note on Buffers.
(a) Phosphate Buffer System.
(b) Bicarbonate Buffer system.
Ans.: (a)
Phosphate Buffer System: This system acts in cytoplasm of all cells consist
of H2PO4 as proton donor and HPO42 as proton acceptor.
H2PO4- H+ + H PO42The phosphate buffer system is effective at pH close to its pka of 6.86 and
thus tends to resist pH changes in range between 6.4 & 7.4, the pH of
intracellular fluids (6.06.9) is nearer to pKa of phosphate buffer &
therefore buffering capacity of phosphates buffer is highly elevated inside
the cells.
In case the ratio of [HPO42] / [H2PO4-] tends to be changed by formation of
more H2PO4- for which the ratio ultimately remains unaltered.
(b)
Bicarbonate Buffer System: this is main extra cellular buffer system

which provides means for removal of CO2 produced by tissue metabolism.
It is the main buffer system in blood plasma and consists of carbonic acid
as proton donor and Bicarbonate as proton acceptor.
H2CO3 H+ + HCO3K1 =
[H + ][HCO3 ]
[H 2CO3 ]
One of its components H2CO3 [Carbonic acid] formed from dissolved CO2
& H2O.
CO2 (d) + H2O H2CO3
K2 =
[H 2 CO3 ]
[CO3 (d)][H 2O]
Also, CO2 (g) CO2 (d)

The pH of bicarbonate buffer system depends on concentration of H2CO3.
The concentration of H2CO3 depends on concentration of dissolved CO2
which in turn depends on concentration of CO2 in gas phase.
Q.11 Explain titration of a weak acid by a strong base with help of titration curve?
36
Ans.: The concentration of acid in original solution can be calculated from volume and
concentration of NaOH added. A plot of pH against amount of NaOH added
reveals pKa of weak acid.
Equilibrium constant for ionization reaction are called dissociation constant ka,
pka which is analogous to pH can be given by
pKa = log
1
= - log Ka
Ka
Titration curve reveals property of acids and their conjugate base.

When acetic acid is titrated with NaOH, the greatest changes in pH takes place at
beginning of and end of titration. The region of least change occurs at mid point
of titration. When exactly 0.5 equivalents of base have been added at this point
concentration of undissociated acid CH3 COOH or HA is equal to its anion (CH3
COO- or A-). At these particular concentrations of HA and A- , the pH {4 .6} is
equal to pKa.
After the addition of each increment of NaOH to acetic acid solution, the pH of
mixture is measured. This value is plotted against fraction of total amount of
NaOH required to neutralize acetic acid. The points so obtained yield titration
curve.
CH3COO-
[CH3 COOH] = {CH3 COO-]
pH 5.26
5
pH
Buffering region
PH = pKa = 4.76
PH = 4.26
2
1
0
0.5
1.0
(OH) equivalents
Biochemistry-I
37
At mid point of titration concentration of proton donor and acceptor are equal
and is called screened zone, is useful region of buffering action.
38
Chapter-2
Biomolecules
Q.1 Which of the following is not a reducing sugar?
A) Glucose
B) Fructose
C) Galactose
D) Sucrose
E) Lactose
Ans.: D) Sucrose
Q.2 The general formula of monosaccharides is
A) CnH2nOn
B) C2nH2On
C) CnH2O2n
D) CnH2nO2n
Ans.: A) CnH2nOn
Q.3 Polysaccharides are
(A) Polymers
(B) Acids
(C) Proteins
(D) Oils
Ans.: (A) Polymers
Q.4 Two sugars which differ from one another only in configuration around a single carbon
atom are termed
(A) Epimers
(B) Anomers
(C) Optical isomers
(D) Stereoisomers
Ans.: (A) Epimers
Q.5 The number of isomers of glucose is
(A) 2
(B) 4
(C) 8
(D) 16
Ans.: (D) 16
Biochemistry-I
39
Q.6 Starch is a
(A) Polysaccharide
b(B) Monosaccharide
(C) Disaccharide
(D) None of these
Ans.: (A) Polysaccharide
Q.7 Number of asymmetric carbon atom in glucose is:
A. One
B. Two
C. Three
D. Four
Ans.: D. Four
Q.8 Monosaccharides can be seperated by:
A. Electrophoresis
B. Chromotography
C. Salting out
D. None of the above
Ans.: B. Chromotography
Q.9 Alpha-D-Glucuronic acid is present in:
A. Hyaluronic acid
B. Chondrointin sulphate
C. Heparin
D. All of the above
Answer: C. Heparin
Q.10 Maltose can be formed by hydrolysis of:
A. Strach
B. Dextrin
C. Glycogen
D. All of the above
Answer: D. All of the above
Q.11 Write two examples of each Disaccharides and Trisacchharides Ans.: Disaccharide - Sucrose, Maltose
Trisaccharide - Raffinose, Rhaminose
Q.12 Give example of Reducing Sugars and Non-reducing Sugar.
40
Ans.: Reducing Sugar Glucose

Non Reducing Sugar Sucrose
Q.13 Define Carbohydrates?
Ans.: Carbohydrates are polyhydroxy aldehydes or ketones and their derivatives also
known as sugars or saccharides.
Q.14 What are Polysaccharides?
Ans.: Polysaccharides are sugars that yield more than 10 molecules of monosaccharide
on hydrolysis; their general formula is (C6H10O5)X.
They are of two types:
(a)
Homo Polysaccharide
(e.g. Starch, Glycogen)
(b) Hetero Polysaccharides

(e.g. Hyaluronic Acid, chondrotin)
Q.15 What are Enantiomers?

Ans.: The two D and L forms of a compound constitute a pair of enantiomers or
enantiomorphs. Enantioners are optically active stereoisomers which are mirror
images of each other.
Q.16 DGlucose is
(a)
Dextrorotatory
(c)
Both
(b)
(d)
Levorotatory
None
Ans.: (a)
Q.17 Write reaction of Fehlings Reagent with Reducing Sugar?

Ans.: C6H12O6 + 2Cu (OH) 2
Glucose
Fehlings
Solution
Gluconic Acid
+ Cu2O +
Cuprous Oxide
(Red Color)
H2O
Q.18 What is difference between reducing and non reducing sugars?

Ans.: Carbohydrates with free aldehyde (at C-1) or free ketone at (C-2) group are called
reducing sugars, and if aldehyde or ketone group is not free but instead utilized
in bond formation is called non reducing sugar.
Q.19 What are disaccharides and how they are classified?
Ans.: Disaccharides are most common oligosaccharide and yield 2-10 monosaccharides
on hydrolyses.
Biochemistry-I
41
Disaccharides
Non reducing
C1 C1 glycosidic
Reducing
C1 C2 glycosidic
C1 C4 glycosidic
C1 C6 glycosidic
linkage
linkage
linkage
linkage
e.g.
Sucrose
Maltose
Melibiose
Trohalose
Q.20 Explain structure and properties of any one disaccharide.

Ans.: Sucrose is disaccharide and is widely distributed in photosynthetic Plants.
In plants molecule of water form glycoside of hydroxyl groups or (- 1) glucose
and B D, Fructose.
It is white crystalline solid, soluble in water and with melting point 180 C.
It is dextrorotatory and is non-reducing sugar.
Structure
6CH2OH
5
H
OH
OH
3
H
H
H
CH2OH
1
H
2
OH 5
OH
OH
Glucose Moeity
CH2OH
H
Frutose Moeity
Fig. : Sucrose
Upon hydrolyses Sucrose yields equimolar. Mixture glucose and fructose which
is often called a revert sugar.
C12H22O11 + H2O
C6H12O6 + C6H12O6
42
Sucrose
water
Glucose
Fructose
On hydrolysis sucrose gives mixture of equimolar quantities of D (+) glucose

(dextrorotatory) and D (-) fructose levorotatory.
This mixture is also called as invert sugar and reaction inversion of sucrose is
catalyzed by enzyme invertase.
Q.21 What is Glycogen or animal starch?
Ans.: Major reserve food in animals often called as animal starch. Glycogen is stored in
liver and muscles of animals. It is branded clean Polysaccharide, whose molecular
weight is 1-2 x 107.
It is white powder and Soluble in water. It is non reducing sugar. On incomplete
hydrolysis it yields Maltose and on complete hydrolysis by acids it gives Glucose.
(C6H10O5)n + (n 1) H20 n (C6H12O6)
Glycogen
n 1 water
n glucose mole cutes

(soluble)
Q.22 Polymers of amino acid are?

(a)
Proteins
(b)
Carbohydrates
(c)
Lipids
(d)
Peptide
Ans.: (a)
Proteins
Q.23 Which form of amino acids are commonly found in Eukaryotes?

(a)
D form
(b)
D & L form
(c)
L form
(d)
None
Ans.: (c) L- form [L = laevorotatory]

Q.24 How many standard amino acids are present?
(a)
20
(b)
30
(c)
10
(d)
15
Ans.: (a)
Q.25 Amino acids are:

(a)
Polar
(b)
Non Polar
(c)
Uncharged
(d)
Amphoteric
Ans.: (d)
Biochemistry-I
43
Q. 26 An example of chromoprotein is
(A) Hemoglobin
(B) Sturine
(C) Nuclein
(D) Gliadin
Ans.: (A) Hemoglobin
Q.27 Casein, the milk protein is
(A) Nucleoprotein
(B) Chromoprotein
(C) Phosphoprotein
(D) Glycoprotein
Ans.: (C) Phosphoprotein
Q.28 Two amino acids of the standard 20 contain sulfur atoms. They are:
a. cysteine and serine
b. cysteine and threonine
c. methionine and cysteine
d. methionine and serine
e. threonine and serine
Ans.: c. methionine and cysteine
Q.29 A peptide bond forms by:
a). a condensation reaction.
b). dehydration synthesis.
c). the formation of a covalent bond.
d). all of these.
Ans.: d) all of these
Q.30 The level of protein structure represented by the alpha-helix shape is
A. primary.
B. secondary.
C. tertiary.
D. quaternary.
Ans.: B. secondary.
Q.31 Proteins may denature when
A. pH is changed.
B. oxygen is present.
C. they form enzymes.
D. substrate concentration is increased.
Ans.: A) pH is changed.
Q.32 When a protein loses its normal three-dimensional configuration, it is said to be
A. saturated.
B. denatured.
C. neutralized.
D. synthesized.
Ans.: B. denatured.
44
Q. 33 Write general structure of amino acid?

Ans.:
COO -
Carboxyl group
Carbon or chiral center
H3N+
(side Chian)
Amino Group
Q.34 Give structure of any five amino acids with nonpolar, aliphatic R group?
Ans.:
COO H3N+
COO H
H3N+
CH3
Glycine
Alanine
COO H3N
CH
CH3
CH3
Valine
COO -
COO -
Biochemistry-I
45
H3N+
C
H2C
HC
H
+NH2
CH3
H2C
CH2
CH2
CH3
Proline
Isoleucine
Q.35 Give structure of amino acid with aromatic R group?

Ans.:
COO -
H3N+
COO -
CH2
H3N+
COO H H3N+
CH2
CH2
C = CH
NH
Phenylalanine
Tyrosine
Q.36 Write Structures of amino acids with uncharged R groups?

Ans.:
Tryptophan
46
Q.37 Write structures of amino acid with negatively charged R groups.

Ans.:
Q.38 Write structures of amino acid with positively charged R groups.

Ans.:
Biochemistry-I
47
Q.39 What is peptide bond?

Ans.: Polypeptides are linear polymers composed of amino acids linked together by
peptide bonds. Peptide bonds are amide linkages formed when unshared electron
pair & - amino nitrogen atom of one amino acid attacks carboxyl carbon of
another amino acid, has C N bond with partial double bond character that
gives rigid planar configuration. Rotation is permitted only about N C and C
C bond. The bond angles labelled for N C & for C C bond are used as
symbols.
Q.40 Write in detail about Primary, Secondary tertiary and Quaternary structure.
Ans.: Proteins have four levels of structural organisation.
(a) Primary Structure: Primary Structure of polypeptide is its amino acid
sequence and amino acids are linked with peptide bonds. Amino acid
sequence is specified by genetic information.
(b) Secondary Structure: As the poly peptide chain fold it forms certain localized
arrangement with adjacent amino acids which constitute secondary structure.
The most commonly types of Secondary Structure are ;
helix
Pleated sheets
helix: rigid, rod like structure. When a poly peptide chain twists into right
handed helical conformation hydrogen bond form between the N-H group of
each amino acid and carboxyl group of amino acid, 4 residues away.
Pleated sheets: form when two or more poly peptides chain segment line
up side by side. Each individual segment refereed to as strand and is
stabilized by hydrogen bonds that form between the poly peptide back bone
N-H and carboxyl group of adjacent chains.
Anti parallel Sheets
Parallel Sheets
48
helix
(c) Tertiary Structure : Unique three dimensional conformations that globular
proteins assumes as a consequence of various interactions like hydrophobic

interactions, electrostatic interactions, hydrogen bonds, covalent bond
between the side chains of primary structure.
(d) Quaternary Structure: Proteins that consist of two or more poly peptide
chains or subunits are said to have quaternary structure. Poly peptide

subunits are held together by non-covalent interactions e.g.; collagen which is
extra cellular matrix protein.
Q.41 Write short note on organic acids. Explain any one.

Ans.: Organic acid is an organic compound with acidic properties. Most common
organic acid are the carboxylic acids. Organic acids are weak acids and do not
dissociate completely in water.
(1) Acetic Acid
(2) Formic Acid
(3) Citric Acid
(4) Oxalic Acid
Citric Acid: It is hydroxy tribasic and occurs in citrus fruits like lemon and
orange. Lemon juice contains 7-10 % citric acid. It is white crystalline solid exist as
monohydrate & has strong acid test. It has following important uses;
(1)
Used as mordant in dye industry.
(2)
Its magnesium salt as laxative, ferric ammonic citrate in case iron

deficiency & sodium citrate in baby powder milk.
(3)
In preparation of Benedicts solution.
Preparation
(1) C12 H22O11 +H2O Air
Sucrose
CH2 COOH
I
Oxidation
C (OH) COOH
I
CH2COOH
Citric acid
Biochemistry-I
(2)
49
CH2OH
CH2Cl
CHOH
2HCl
CHOH
CH2OH
CH2Cl
Oxidation
H2CrO4
Glycerol
] inter mediate
H3O+
Citric Acid
Reactions: (1) Citric Acid

H2S2O7
Acetone di carboxylic Acid

CO2
Aceto acetic acid
CO2
Acetone
(2) Complex for motion: Alkaline solution of citric acid & copper sulphate
solution in presence of sodium carbonate forms deep blue colored water soluble
complex known as Benedict solution & is used to test aldehydes & reducing
sugars.
Q.42 Give example of Nitrogenous base.
Ans.: (a)
(b)
Purines: - Adenine & Guanine

Pyrimidines : Cytosine ,Uracil, Thymine
Q.43 Write structure of ribose and deoxyribose Sugar?

Ans.:
5
50
HOCH2
H
OH
OH
HOCH2
OH
OH
OH
D ribose
D 2 deoxy ribose
Q.44 Give structure of Pyrimidine bases.

Ans.:
Q.45 Give structure of Purine bases.

Ans.:
Q.46 Write Hydrolytic products of nucleon acid.

Ans.:
NH3 BO(OH)2
Nucleotides
1150
Enzymes(nucleases)
AqNH3
Decreasing
175C
Molecular
Wt
Nucleic
Acid
MgO in SOI4
Biochemistry-I
51
Nucleosides + H3PO4
Heat
Heat
Inorganic Acid
Sugar + Purines + Pyrimidines
Q.47 Give DNA and RNA structure showing phosphodiester bond.
Q.48 Which is insoluble RNA.

(a)
rRNA
(b)
tRNA
(c)
mRNA
(d)
None
Ans.: (a)
Q.49 Which is known as template RNA.

(a)
tRNA
(b)
mRNA
(c)
rRNA
(d)
None
Q.50 Which is Soluble RNA.

Ans.: (b)
with
52
(a)
mRNA
(b)
tRNA
(c)
rRNA
(d)
All
Ans.: (b)
Q.51 Differentiate between Deoxyribonucleic (DNA) and ribonucleic acid (RNA).

Ans.:
S.
No.
DNA
RNA
Found mainly in chromatin of Most RNA is present in cell

cell nucleus.
cytoplasm & little in nucleus.
Never present in free state in May be present in free state.

cytoplasm.
Normally double stranded and Single stranded and rarely

rarely single stranded.
double stranded.
Sugar moiety in DNA is 2- Sugar moiety in RNA is ribose

deoxy ribose which contain a which contains 2- hydroxyl
hydrogen atom at C -2.
group.
Nitrogenous
bases
are Common Nitrogenous base are
Adenine, Guanine, Cytosine Adenine, Guanine, Cytosine
and Thymine.
and Uracil.
The base ratio (A/T and G/C) It

need
not
have
are necessarily around one.
complementary base ratio.
DNA acts as template for its RNA doesnt replicate.

Synthesis.
DNA is usual genetic material.
During base pairing, Adenine In case of pairing, Adenine

pairs with Thymine and Pairs with Uracil and Guanine
Guanine with Cytosine.
with Cytosine.
RNA is genetic material of

some viruses only.
Q.52 Which of following statement is not true for Lipids?

(a)
Esters of Glycerol and Fatty Acids.
(b)
Hydrophobic in nature.
(c)
Insoluble or Poorly Soluble in Water.
(d)
None
Ans.: (d)
Biochemistry-I
53
Q.53 Write four general functions of biological Lipids.

Ans.: (1)
They serve as storage form of metabolic fuel.
(2)
They serve as transport form of metabolic fuel.
(3)
They provide structural components of membranes.
(4)
They have protective functions is bacteria, plants, insects and vertebrates

serving as a part of the outer coating between the body of organism and
the environment.
Q.54 What do you understand by Triacylglycerols?

Ans.: Triacylglycerols are triesters of fatty acids and glycerol, general formula can be
given by.
H2C O C R1
H C O C R2
H2C O C R3
They are non polar, hydrophobic in nature and major form of stored lipid.
Because triacylglycerols have no charge they are some times referred to as neutral
fats. Most triacylglycerol molecules contain fatty acids of varying, lengths which
may be unsaturated, saturated or combination of both.. Fats which are solid at
room temperature contain large proportion of saturated fatty acids. Oils are
liquid at room temperature contain a large proportion of unsaturated fatty acids.
If fats are hydrolyzed with alkali such as NaOH or KOH, soap is produced and
process is called saponification.
Q.55 What are Steroids and Eicosanoids.
Ans.: Steroids are complex derivatives of tri-terpenes. Each type of steroid composed of
four fused rings called steroid nucleus. Sterol is class of steroids characterized by
hydroxyl group at C-3. Cholesterol, an important molecule in animals is example
of sterol. It is and essential component in animal cell membranes. It acts as
precursor for biosynthesis of all steroid hormones, vitamin D & bile salts. Sterol
that is common to plants is stigma sterol and campesterol.
Eicosanoids originated from 20 carbon poly unsaturated fatty acids (eicosanoic
acids), particularly arachidonic acid. It is includes Prostaglandins, thrombaxane
and leukotrienes. They are potent hormones and act locally instead of being
transported in blood to act on cells in other tissues or organs.
54
Q.56 How many carbon atoms are present in plasmatic acid.

(a)
15
(b)
16
(c)
14
(d)
None
Ans.: (a)
Q.57 General Formula for Fatty acid (Saturated).

(a)
CH3 (CH2)n COOH
(b)
CH3 (CH2)n (COOH)2
(c)
CH3 COOH
(d)
None
Ans.: (a)
Q.58 Non essential Fatty acids are synthesized form.

(a)
Acetic Acid
(b)
Acetyl Co A
(c)
Aceto Acetic Acid
(d)
All of above
Ans.: (b)
Q.59 Unsaturated fatty acids have

(a)
Presence of double bonds (b)
Presence of Methyl group
(c)
sp hybridization
All of above
(d)
Q.60 Essential fatty acid:

(A) Linoleic acid
(B) Linolenic acid
(C) Arachidonic acid
(D) All these
Ans.: (D) All these
Q.61 The physical properties of cholesterol are best described as
a. polar, charged.
b. polar, uncharged.
c. nonpolar.
d. amphipathic, charged.
e. amphipathic, uncharged
Ans.: e. amphipathic, uncharged
Q.62 A characteristic common to all lipids is
a). that they contain long chains of C-H bonds.
Ans.: (a)
Biochemistry-I
55
b). that they are insoluble in water.

c). that they have a glycerol backbone.
d). All of these are characteristics of all lipids.
Ans.: b) that they are insoluble in water.
Q.63 A characteristic of unsaturated fats is that they
A. denature as they cool.
B. are made up of glucose and fructose.
C. are made up of amino acids and glycerol.
D. have double bonds in their carbon chains.
Ans.: D) have double bonds in their carbon chains.
Q.64 Which of the following are components of a phospholipid?
A. cholesterol, glycerol, fatty acids
B. fatty acids, phosphate group, glycerol
C.glycerol, amino acids, phosphate group
D. phosphate group, cholesterol, monosaccharides
Ans.: B. fatty acids, phosphate group, glycerol
Q.65 Compared to saturated fats, unsaturated fats contain less
A. oxygen.
B. glycerol.
C. hydrogen.
D. fatty acids.
Ans.: C. hydrogen
Q.66 A lipid molecule is produced when
A. fatty acids bond to glycerol.
B. amino acids bond to glycerol.
C. monosaccharides bond to glycogen.
D.dehydration occurs between fatty acids and glycogen.
Ans.: fatty acids bond to glycerol.
Q.67 Lipids are composed of
A. nucleotides.
B. amino acids.
C. monosaccharides.
D. glycerol and fatty acids.
Ans.: D. glycerol and fatty acids.
56
Q.68 What are phospholipids? Write about different types of phospholipids.

Ans.: Phospholipids are amphipathic molecules abundantly found in plasma
membrane. There are two types of phospholipids:
(a) Phosphoglycerides (b) Sphingo phospholipids
(A) Phosphoglycerides or Glycero phospholipids: Are molecules that contain
glycerol, fatty acids, Phophate and an alcohol (e. g. Choline) Phosphoglycerides
are most numerous phospholipids molecules found in cell membranes. The
simplest phophoglyceride is phosphatidic acid composed of Glycerol-3 phosphate
that is esterified with two fatty acids. Phosphoglyceride molecules are classified
according to which alcohol becomes esterified to phosphate group for example if
alcohol is choline, the molecule is called phosphatidylcholine and if serine called
phosphatidylserine.
(B) Sphingo phospholipids: Contain long chain amino alcohol called
Sphingosine instead of Glycerol. When amino group of Sphingosine is acylated
with fatty acid, the product is ceramide which is structural parent of all
Sphingolipids.
Glycosphingo lipid: In glycosphingolipid head group contains one or more
sugars connected directly to OH at C -1 of ceramide moiety.
(1)
Cerebroside: Have single sugar linked to ceramide.
(2)
Globoside: With two or more sugars.
(3)
Gangliosides: A complex glycophospholipid that contain oligo saccharide
as their polar head groups and one or more residues of N-acetyl
neuraminic acid and sialic acid.
Selected Sphingo lipid Storage Diseases:
S.
No.
Name
Accumulating
Sphingolipid
Symptom
Tay Sachs Ganglioside

disease
Blindness, mental retardation.
Gauchers
disease
Livers and spleen enlargement,

mental retardation.
Glucocerebroside
Biochemistry-I
57
Section-C
Chapter-1
Nucleus and Heredity

Q.1
Okazaki fragments are also known as:

(a)
Leading Strand
(b)
Lagging Strand
(c)
Both
(d)
None
Ans.: (b)
Q.2
Semi Conservative mechanisms was demonstrated by:

(a)
Meselson & Stahl
(b)
Watson & Crick
(c)
Both
(d)
None
Ans.: (a)
Q.3
(a)
Column Component
(b)
Luminal Component
(c)
Annular Component
(d)
All of above
All of above
Gene is (a)
Nucleoside sequence
(b)
Chromosome
(c)
DNA
(d)
Nucleotide sequence
Ans.: (d)
Q.5
Meselson & Stahl
Nuclear pore complex contain:
Ans.: (d)
Q.4
Lagging Strand
Nucleotide sequence
RNP stands for:

(a)
Ribo Nuclear Protein
(b)
Ribosome Nuclear Protein
(c)
Ribo Nucleolar Protein
(d)
None
58
Ans.: (a)
Q.6
Ribo Nuclear Protein
3 5 Proofreading is required for:

(a)
Replication Fidelity
(b)
Replication error
(c)
Both
(d)
None
Ans.: Replication Fidelity

Q.7
Eukaryotic RNA Polymerase I is present in:

(a)
Nucleolus
(b)
Nucleus
(c)
Cytoplasm
(d)
Mitochondria
Ans.: (a)
Nucleolus
Q.8
UREs are known as:

(a)
Upstream Regulating Elements
(b)
Upstream Regulatory Elements
(c)
Both
(d)
None
Ans.: (b)
Q.9
Upstream Regulatory Elements
Polysomes are:
(a)
Polyribosome
(b)
Poly Nucleosomes
(c)
Both
(d)
None
Ans.: (a)
Polyribosome
Q.10 Ribosome binding site is known as:

(a)
TATA BOX
(b)
Shine Dalgarno Sequence
(c)
UREs
(d)
None
Ans.: (b)
Shine Dalgarno Sequence
Q.11 How many initiation factors are present in Prokaryotes?

(a)
(b)
Biochemistry-I
(c)
Ans.: (c)
59
(d)
Q.12 Which of the following is Eukaryotic releasing factor (RF).

(a)
e RF (a)
(b)
e RF ATP
(c)
e RF G
(d)
e RF
Ans.: (d)
e RF
Q.13 Translational Elongation is associated with:

(a)
Amino acyl tRNA delivery
(b)
Peptide bond formation
(c)
Translocation
(d)
All of above
Ans.: (d)
All of above
Q.14 Which of the following is start codon:

(a)
AUG
(b)
GUG
(c)
AAA
(d)
None
Ans.: (a)
AUG
Q.15 Which of the following is translocase:

(a)
(EF G)
(b)
RF 1
(c)
EF TU
(d)
EF TS
Ans.: (a)
(EF G)
Q.16 Write short note on Nuclear membrane Y Nucleopore complex.

Ans.: a) Structure: Nuclear envelop encloses the DNA & defines the nuclear
compartment. It is formed of two membranes. The inner membrane contains
specific proteins that act as binding sites for nuclear lamina that supports it. The
inner membrane is surrounded by outer nuclear membranes which closely
resemble outer membrane of Endoplasmic reticulum. In between outer and inner
nuclear membrane space present is called perinuclear space Nuclear envelop in
all Eukaryotes is perforated by nuclear pores. Each pore is formed by large
elaborate structure known as nuclear pore complex.
Each pore complex contains one or more open aqueous channels through which
water soluble molecules that are smaller in size can diffuse.
60
In cross section the nuclear pore complex appears and composed of:
(1)
Column component which forms the bulk of pore wall.
(2)
Annular component which extend spokes toward centre of the pore.
(3)
Luminal component which is formal by large trans membrane

glycoprotein that is thought to help anchor the complex to nuclear
membrane. On nuclear side the fibrils converge to form cag like structure.
Protein & RNA molecules bind to specific receptor protein located in pore
complexes are actively transported across the nuclear envelop through
complexes.
Q.17 Describe Packaging of DNA?
Ans.: Gene is defined as nucleotide sequence in a DNA molecule that acts as functional
unit for production of an RNA molecule. A chromosome formed form single
enormously long DNA molecule that contain set of many genes.
Eukaryotic chromosomes contain a long linear DNA molecule which must be
packaged into nuclear. The name chromatin is given to highly ordered DNA
protein complex which makes up Eukaryotic chromosomes. The chromatin
structure serves to package & organize chromosomal DNA & is able to alter its
level of packing at different stages of cell.
Biochemistry-I
61
The major components of chromatin are histones small basic proteins which bind
tightly to DNA. There are four families of core histones, H2A, H2B, H3 H4 & H1
which has some different properties & distinct role.
Nucleosome core is the basic unit of chromosomes structure, consisting of protein
octamer containing two each of core histones with 146 bp of DNA wrapped
around it. A single molecule of H1 organizes DNA between nucleosomes. A
nucleosome core plus H1 is known as chromtosome.
Chromatin is organized into larger structure, known as 30nm fibre or Solenoid,
thought to consist of a left handed helix of nucleosome with approximately 6
nucleosomes per helical turn. Most chromatin exists in this form.
On the higher order structure chromosomal DNA is organized into loops of up to
100 Kb in form of 30mm fiber. The over all structure save what resembles that of
the organizational domains of prokaryotic DNA.
62
Q. 18 Comment DNA as a genetic material .

Ans.: DNA is found to be the genetic material in almost all living beings except some
plant viruses.
Evidences of DNA as genetic material.
(1)
Bacteria Transformation: By Frederick Griffith provided first clear

evidence that DNA is hereditary material while working with
Pneumonia causing bacteria. He conducted following set of experiments.
Biochemistry-I
(1)
63
Virulent strain culture inject mice Death
Virus Recovered
(2)
Non Virulent strain culture inject mice Lives
No Virus Recovered
(3)
Virulent strain Heat Killed inject mice Lives
No Virus Recovered
(4)
Virulent strain (Heat killed) + non virulent inject mice Death
Virus Recovered
Conclusion: presence of heat killed Virulent strain has caused transformation of

nonvirulent bacteria into Virulent called bacterial transformation.
(2)
Three Scientists Avery Macleod & Mc. Cartey recognized the principle for
converting non virulent to virulent and found it to be DNA.
(3)
Lederberg and Tatum showed that conjugation results in transfer of

genetic material (DNA) from one to other. During conjugation cytoplasmic
bridge is formed between conjugated bacteria & DNA transferred was
found to be vary with period of conjugation. Also, length of DNA &
amount of genetic information transferred are directly related.
(4)
Hershey along with Luria and Dulbruck discovered phage lytic cycle &
demonstrate that DNA enters the host cell and act as hereditary or genetic
material.
Following above experiments demonstrate that DNA is the genetic
material and is responsible for careering genetic information.
Q.19 Describe DNA Replication in Prokaryotes and Eukaryotes.

Ans.: Transmission of chromosomal DNA from generation to generation is crucial to
cell propagation. This can only be achieved when chromosomal DNA is
accurately replicated, providing two copies of the enter genome for distribution
in each daughter cell.
(A)
Semi Conservative Replication: If the two strands of parental double helix

of DNA separated, the base sequence of each parental strand could serve
as template for synthesis of new, complementary producing two identical
64
progeny double helices. This process is called Semi Conservative

Replication because the parental double helix is half conserved each
parental strand is remaining intact.
(B)
Unidirectional and Bidirectional DNA Replication: all known DNA

molecules, with only few exceptions replicate as circles & hence initiate
within the helix. DNA replication doesnt start at random locations but at
particular sites called origins of DNA replication. A DNA whose
replication starts from an origin and proceeds bidirectionally or
unidirectionally to terminals site is called replicon. In each replicon
replication is continuous from origin to terminus & associated with
movement of replication point called Replication fork. In bidirectional
replication both ends of replication fork are moving. Where as in
unidirectional replication one of two ends of replication end remains
stationary and other end serve as replication fork and moves with
replication. An example of unidirectional replication is replication of
mitochondrial DNA.
(C)
Enzymes for DNA Replication: Different prokaryotic and Eukaryotic cells

have been found to contain three kinds of nuclear enzymes that act on
DNA namely nucleases, polymerases and ligases.
(I)
Nuclease Enzyme: The Nuclease Enzyme act to hydrolyze or break down

a polynucleotide chain into its component nucleotides. A polynucleotide is
held together by 3, 5 phosphodeister bond and nuclease enzyme will
attack either the 3 or 5 end of linkage.
(a)
Exonuclease Enzyme: Exonuclease enzyme which begins attack at 3 OH

and 5 P end of polynucleotide is called exonuclease.
(b)
Endonuclease Enzyme: Endonuclease enzyme also attacks one of the two

sides of phophodiester linkages but react only with those bonds that occur
within the interior of Polynucleotide chain.
(II)
Polymerase or replicase Enzyme: It catalyses the formation of a polymer.

A polymerase enzyme is called replicase enzyme, brings about
chromosome replication.
Prokaryotic DNA polymerases: Three different DNA polymerases are known in

E. coli and other prokaryotes of which DNA polymerase I and II are mean for
DNA repair DNA Pol III for actual DNA replication.
(a)
DNA polymerase I: isolated by Arthur Kormberg and known

is Kornberg enzyme. This enzyme has template site, primer site at 3
cleavages or Exonuclease site. DNA Pol is involved in removing RNA
primers form Okazaki fragment and filling gap due to its 5 3
Biochemistry-I
65
polymerase capacity. Both polymerization & exonuclease activity DNA

polymerase I is called as proof reading or editing function.
(b)
DNA Pol II: It is DNA repair enzyme & brings about growth in
5 3 direction using 3 OH groups.
(c)
DNA Pol III: Plays essential role in DNA replication. It is multimeric

enzyme having the Subunits, all having different functions.
(d)
DNA Ligases: Capable of catalyzing phosphodiester bond formation

between 3 OH and 5 P group of a nick of DNA. This is created by
endonuclease enzyme there by restoring and DNA duplex.
(III)
RNA Primers in DNA replication: DNA polymerase cannot initiate

synthesis of DNA without availabity of a primer strand. Short RNA
oligonucleotide segments called RNA primers have to be synthesized by
DNA primase. The primers are about 10 nucleotides. In bacteria two
different enzymes are known to synthesize primer RNA oligonucleotides
RNA polymerase (on leading strand) & DNA primase on lagging strand.
(D)
Proteins involved in opening of DNA helix :
(I)
DNA helicases: Are ATP dependent unwinding enzymes which promote

separation of the two parental strands and establish of replication fork
unwinding of template DNA helix. At replication fork two DNA helicases
act, one running along the leading strand and other along lagging strand.
(II)
Single strand DNA binding proteins: Behind the replication fork the
Single DNA strands are prevented from rewinding about one another (or
forming double stranded hair pin loops in each Single Strands) by action of
Single Stranded Binding Proteins. SSB proteins bind to exposed DNA
strands without covering bases which there fore remain available for
templating process.
(III)
DNA GYRASE: The action of helicase introduces a positive Super coil into
Duplex DNA ahead of replication fork. Enzyme called topoisomerase relax
the super coil by attaching to transiently super coil Duplex nicking one of
the strand and rotating it through the unbroked strand, the nick is then
resealed.
Topoisomerase I : cause single strand break or nick which allow two sections of
DNA helix on either side of nick to rotate freely relative to each other using
phosphodiester bond in strand opposite the nick.
Topoisomerase II: Forms covalent bond to both strands of DNA helix at the same
time making transient double strand break in helix.
66
Replication of DNA in Prokaryotes:

(1)
Initiation of DNA replication : Comprising three steps :
(i)
Recognition of the origin. (0)
(ii)
Opening of DNA duplex to generate a region of single stranded DNA.
(iii)
Capture of Dna B protein (5 3 helicase)
Dna A ATP complex binds at 9bp inverted repeat regions of ori. C of E coli
and provides opening of DNA duplex in a region of 3 direct repeats of 13 bp
sequence. The opening occurs form 13 mer left wards and requires negatively
super coiled DNA and HU proteins. Dna B is transferred to exposed single
stranded DNA & cause unwinding of DNA in presence of ATP, SSB protein and
DNA gyrase. This result in unwinding of DNA duplex & replication from origin
proceeds in both directions.
(2)
(i)
(iii)
(v)
(vii)
Elongation of DNA chain: This step requires presence of following

enzymes.
Helicase
(ii)
Primase
DNA polymerase Holo enzyme
(iv) SSB Protein
RNAS H
(vi) DNA polymerase I
Ligase
(1)
Helicases travel in 5 3 direction it generates a replication fork by

opening DNA duplex.
(2)
DNA strand having heliase become lagging strand .DNA primase

associates with helicase forming primosome which synthesize multiple
primers for lagging strand & single RNA primer for leading strand.
(3)
For synthesis of lagging strand, DNA pol III has to work on some strand to
which DNA B helicase is bond but it travels in opposite direction, helicase,
primase and DNA pol III work together in strand elongation.
Primase is taken up from solution and is activated by helicase to synthesise a

RNA Primer strand & utilized for synthesis of precursor okazaki fragments. On
completion of okazaki fragments the RNA primer are excised by DNA pol I
which then fills the gap .DNA ligase forms phosphodiester bond. That links the
free 3 end of primer replacement of 5end of okazaki fragments.
In bidirectional DNA replication the leading strand is primed once on each of
parental strand. RNA primer of leading strand is synthesized by RNA
polymerase enzyme DNA pol III cause elongation of leading strand & finally
DNA pol I and ligase enzyme give final to touch to leading strand.
Biochemistry-I
67
Eukaryotic DNA polymerase: Eukaryotes found to contain following 5 types of

Polymerase.
(i)
DNA Pol : Cytoplasmic polymerase
(ii)
DNA Pol : Nuclear polymerase
(iii)
DNA Pol : Mitochondrial polymerase.
(iv)
DNA Pol : Found in mammalian cell and is PCNA dependent for DNA
synthesis possessively.
(v)
DNA Pol : Found in budding yeast & hela mammalian cell.
Eukaryotic DNA replication requires two different DNA polymerase enzymes

namely DNA Pol &DNA Pol . DNA Pol synthesizes the DNA on leading
strand where as DNA polymerase synthesizes the DNA on lagging strand.
Several other factors are also involved in eukaryotic DNA replication.
Before onset of DNA synthesis there is presynthelic stage 8 10 Minutes duration
for formation of unwound DNA Duplex. This step needs only 3 purified proteins,
namely T antigen, RF A & Topoisomerase I & II .T antigen using its DNA
binding domain forms a multi subunit complex with site in presser of AIP &
cause local unwinding.
More extensive duplex unwinding occurs due to association of RF A &
Topoisomerase with help of helicase component help in unwinding of DNA by
altering topology of DNA at replication fork. RF A or SSB proteins bind to
unwound single stranded DNA. The primer RNA synthesis is formed by primase
which is tightly associated with DNA polymerase . DNA Pol helps in synthesis
of okazaki fragment in 5 3 direction. RF C & PCNA help in switching DNA
polymerase so that Pol is replaced by Pol which is then continuously
synthesized on the leading strand. Another okazaki fragment is then synthesized
from replication fork on lagging strand by Pol -primase complex & this step is
repeated again and again till entire DNA molecules is covered.
RNA primers are removed and gaps all filled as in prokaryotic DNA replication.
The small size of eukaryotic lagging strand fragments appears to reflect the
amount of DNA wound from each nucleosome as fork progresses. In addition to
doubling the DNA, the histone content of cell is also doubled during S phase.
Q.20 What is CENTRAL DOGMA?
Ans.: There is unidirectional flow of genetic information form DNA through RNA to
Protein is that is DNA makes RNA which makes protein.
Replication
DNA
RNA
68
Transcription
Reverse Transcription
RNA editing
RNA replication
Translation
The flow of genetic information

Q. 21 Give Detail account an Prokaryotic & Eukaryotic Ribosomes.
Ans.: Prokaryotic Ribosomes: Ribosome are complexes of r RNA and specific
ribosome proteins and other large RNPs are the machines the cell uses to carry
out translation. The E coli 70 S ribosome is formed from large 50 S and small 30 S
diff proteins and one each of 235 and 5S r RNA. The small subunit contains 16 S r
RNA molecule and 21 different proteins.
Eukaryotic Ribosome : Are larger and complex then their prokaryotic
counterparts but carry out the same role. The complete mammalian 80s ribosome
is composed of one large 60 S subunit some small 40 S. subunit. The 40 S subunit
contains 18 S r RNA molecule and about 3 destruct proteins. The 60 S subunit
contain one 5 S r RNA, one 5 8 S r RNA one 28 S r RNA and about 45 proteins.
31 Proteins
+
50 S
23 S RNA
70 S
5 S RNA
+
30 S
2.75 x 106 Da
.95 x
106
Da
Ribosome
Subunit
1.7 x 106 Da
21 Proteins
+
16 S RNA
Protein &
RNA
Biochemistry-I
69
Prokaryotic Ribose
45 Proteins
+
28 S RNA 5.8 S RNA
5 S RNA
60 S
80 S
40 S
Ribosome
Subunit
30 Proteins
+
18 S RNA
Protein &
RNA
Eukaryotic Ribosome
Q. 22 Write short note on mechanism of protein syntheses?
Ans.: There are three stages of protein synthesis;
(1)
Initiation: The assembly of ribosome on mRNA.
(2)
Elongation: Repeated cycles of amino acid delivery, peptide bond

formation and movement a long mRNA (translocation).
(3)
Termination: The release of polypeptide chain.
Initiation: In prokaryotes, initiation requires the large and small ribosome

subunit the mRNA, the initiator t RNA, three ignition factors (IF s) and GTP, IF1
and IF3 bind to 30 S subunit and prevents the large subunit binding. IF2 + GTP
can their bind & will help initiator t RNA to bind later. This small subunit
complex now attach to mRNA via its ribosome binding sites. The initiator t RNA
can then base pair with AUG initiation colon which release IF3 thus creating 30 S
initiation complex the large subunit then binds, displacing IF 1 and IF2 + GDP
giving 70 S initiation complex which is fully assembled ribosome at corrected
position on mRNA.
Elongation: Involves the three factors (EFs), EF Tu, EF Ts & EF G, GTP
charged t RNA and 70 S ignition complexes. It takes place in three steps.
(1)
A charge t RNA is delivered as complex with EF Tu and GTP. The GTP is

hydrolyzed and EF Tu GDP is released which can be reused with the
help of EF Ts & GTP.
70
(2)
Peptides transferees make peptide bond by joining the two adjacent amino
acids without the input of more energy.
(3)
Translocase (EF G), with energy form GTP moves the ribosome one colon
along the mRNA, ejecting the uncharged t RNA and transferring the
growing peptide chain to P sites.
Termination: Release factors (RF1 or RF2) recognize stop codons & helped by RF3
make peptides transferase join the polypeptide chain to water molecules, thus
releasing it. Ribosome release factor helps to dissociate the ribosome subunits
form the mRNA.
Most of the differences in mechanism of protein syntheses between prokaryotes
and eukaryotes occur in initiation stage however, eukaryotes have just one release
factor (eRF). The eukaryotic initiator t RNA doesnt become N formatted as in
prokaryotes.
The eukaryotic 40 S ribosome subunit complex binds to 5 cap region of the
mRNA complex and moves along it looking for an AUG start colon.
Biochemistry-I
71
Translation summary in prokaryotes.

Initiation: This major point of difference between prokaryotic & eukaryotic
protein synthesis there being at least nine eIFs involved functionally this factor
can be groups they either bind to ribosome subunits or to the m RNA deliver the
initiator t RNA or displace other factors. In contrast to the event in prokaryotes
initiation involves the initiator t RNA biding to 40 S subunit before it can bind to
mRNA phophorytation of eIF2 which delivers the initiator tRNA, is an important
control point.
Elongation: This stage of protein Synthesis is essentially identical to that
described for prokaryotes. The factors EF Tu, EF Ts & EF G have direct
72
eukaryotic equivalents called eEFl , eEFl , & eEF 2 respectively which carry
out the same roles.
Termination: Eukaryotes use only one release factor (eRF), which requires GTP,
for termination of protein synthesis. If can recognize all there stop colons.
Translational Control: In prokaryotes the level of translation of different citrons
can be affected by;
(1)
Binding of short antisense molecules.
(2)
Relative stability to nuclease of parts of polycistronic mRNA.
(3)
Binding of proteins that prevent ribosome access.
In Eukaryotic protein binding can also mask the mRNA, prevent translation &
repeats of sequence 5 AUUUA 3 can make mRNA unstable and less frequently
translated.
Protein Targeting : The signal sequence of secreted proteins causes the
translating ribosome to bind factors that make the ribosome dock with membrane
and transfer the protein through the membrane as it is synthesized usually the
signal sequence is then cleaved off by signal peptidase.
Protein modification: The most common alterations to nascent polypeptides all
those of cleavage and chemical modification. Cleavage accurse to remove signal
peptides to release mature fragments from poly proteins to remove internal
peptides as well as trimming both N & C termini often Phosphorylation controls
activity of protein.
Protein degradation: Damaged modified or inherently unstable proteins are
marked for degradation by having multiple molecules of ubiquitin covalently
attached. The ubiquitin ylated protein is then degraded by protease complex.
Q. 23 Explain Mechanism of Transcription.
Ans.: Transcription involves following three aspects:
(1)
Enzymatic synthesis of RNA.
(2)
Signals that determine at what point on DNA molecule transcription start

& stop.
(3)
The types of transcription product show they are converted to RNA

molecules needed by all.
(I)
Enzymatic synthesis of RNA: Following are the essential characteristics of

synthesis of RNA.
Biochemistry-I
73
(1)
The precursor in synthesis of four ribonucleotide triphosphates ATP, GTP,

CTP & UTP. On ribose portion of each dNTP there are two on groups one
each on 2 & 3 carbonators.
(2)
In polymerization reaction 3 OH group on one nucleotide reacts with 5

tri phosphate of a second nucleotide a pyrophosphate is removed and a
phophodiester bond results.
(3)
Sequence of base in RNA molecule is determined by base sequence of

DNA. The DNA molecule being transcribed is double stranded, only one
strand serve as template.
(4)
RNA chain grows in 5 3 direction; that is nucleotides are added to 3

OH end of growing chain. The RNA molecule is terminated by a 5- tri
phosphate at non growing end. The RNA molecule is autiparallel to DNA
stand being copies. Once initiated RNA chains grow at rapid rate of 40 50
ntd per second.
(5)
RNA polymerase in contrast with DNA polymerase is able to initiate chain

growth that is no primer is needed.
(6)
Only ribonucleoside 5 tri phosphates participate in RNA synthesis & first

base to be laid down in initiation event is a tri phosphate.
Overall Requirements:
XTP First nucleotide at 5 terminus of RNA chain.
NMP Mono nucleotide in RNA chain.
RNA P RNA polymerase
PPi Pyrophosphate released.
Mg+2 required for polymerization.
RNA polymerase Enzyme: In prokaryotes single RNA polymerase is responsible
for all kind of RNAs synthesis. It is one of the largest enzymes known. Consist of
six subunit is (polypeptide chain) two identical alpha () and one chain each of
(), omega () & sigma () subunit. The complete RNA polymerase is termed as
holo enzyme and represented as 2 1 association of factors is not very
firm. Sigma factor helps in recognition of start signals on DNA molecule and
directs RNA polymerase in selecting the initiation sites one RNA molecule
becomes 8-9 bases long factor dissociates & core enzyme brings about
elongation of m RNA.
(II)
Binding of RNA polymerase to Promoter & Initiation: Transcription
doesnt progress along entire length of chromosome only some parts are
transcribed also only one of two strand of DNA are transcribed this strand is
74
called sense strand & the other strand is called antisense strand. RNA is
synthesized in 5 3 direction localized unwinding move along molecules
followed by recoiling of the helix behind the nearly synthesized RNA. The region
of sense strand of DNA which is transcribed into RNA is called coding region.
The first step in initiation is binding of RNA polymerase to DNA molecules.
Binding occurs at particular sites PROMOTERS which are specific sequences of
20 200 bases. Two special promoter regions have been identified:
(1)
Pribnow box: Consensus sequence region of fine to ten bases preceding

the coding region. Consensus sequence is TATAATG.
(2)
Hogness box : In Eukaryotes the same region has the sequence :
TATAAAT Also known as TATA BOX. It is region in which double helix opens
to form open promoter complex.
Another important region further upstream from TATA BOX is 30-35 bases form
coding region called -35 sequence or recognition sequence. Subunit first binds
to -35 sequences in a highly specific interaction and then, appropriate region
some in contact with -10 sequence of pribnow box.
The open promoter complex has local unwinding of DNA helix. The base
composition of sequence of pribnow box is A + T rich makes DNA strand to open.
Elongation: Once an open promoter complex has formed, RNA polymerase is
ready to initiate RNA synthesis. RNA polymerase contains two nucleotides
binding sits called initiation site and elongation site. The initiating nucleoside tri
phosphate binds to enzyme in open promoter complex and forms hydrogen
bond. The elongation site is then filled with
Nucleoside tri phosphate & the two nucleotides are joined together first base is
released from initiation site and initiation is completed.
The elongation phase begins when polymerase releases the base & then moves
along the DNA chain. After several nucleotides are added to growing chain RNA
polymerase changes its structure and form stable ternary elongation complex. The
core enzyme moves along the DNA binding nucleoside tri phosphate that can
pair with next DNA base & open the DNA helix as it moves thus during
elongation phase addition of 40 bases per second at 37C takes place. The nearly
synthesized RNA is released form its hydrogen bonds with DNA as helix
reforms.
Termination : RNA synthesis termination occurs at specific base sequence in
DNA molecule Termination region consist stein loop configuration or G + C rich
region or sequence of A. T pairs that yield in RNA sequence 6 to 8 waits followed
by adenine.
Biochemistry-I
75
In fact there are two types of termination event those that depend only on DNA
base sequence & those that require the presence of termination protein called
shop.
Eukaryotic Transcription: For Eukaryotic transcription the regulatory DNA
sequences for genes transcribed by each of three RNA polymerase differ.
Initiation: Various transcription factors are also involved in formation of
transcription complex. Each RNA polymerase is believed to have its own set of
transcriptions factors.
Transcription factors can be defined as proteins which are needed for initiation of
transcription. They help in DNA binding of a RNA polymerase and constitute so
called Pre Initiation Complex.
(a)
Formation of Transcriptosome: A promoter sequence which is responsible

for generic promoter. Initiation of transcription generic promoter by RNA
polymerase II require following set of transcription factors :
(i)
TF II D binds at TATA box.
(ii)
The (i) step permits the association of TF II A & TF II B.
(iii)
TF II B forms so called DB complex and RNA Polymerase II associates to

promoter site.
(iv)
RNA pol II is facilitated toward promoter TF II F to form transcription

complex.
(v)
Orderly addition of TF II E, TF II H and TF II j helps the initiation process.
Elongation: There are certain accessory proteins of transcription called elongation

factors which over all enhance the activity of RNA polymerase II and lead to
increase is the elongation rate. At least two such proteins are known.
(i)
TF II F accelerated RNA chain growth relatively uniformly in concord with

RNA Polymerase II.
(ii)
The TF II S helps in elongation of RNA chain by unburdening the

obstruction in path of such elongation. TF II S is known to act: by first
causing hydrolytic cleavage at 3 end of RNA chain there by helping in
forward movement of RNA polymerase through any block to elongation.
Termination: In Eukaryotes, the actual termination of RNA polymerase II

activity during transcriptions may take place through termination sites similar to
those found in prokaryotes.
However, the nature of individual sites is not known. Such termination sites are
believed to be present away. (Sometimes up to one kilo base away from the site of
the 3 end of m RNA)
76
Transcription by RNA polymerase
Biochemistry-I
77
Chapter-2
Mitochondria and Release of Energy

Q.1
Mitochondria Contain
(a)
Outer Membrane
(b)
Inner Membrane
(c)
Inter Membrane
(d)
Matrix
(e)
Ans.: (e)
Q.2
All of above
All of above
Mitochondria Contain Enzymes for

(a)
Citric Acid Cycle
(b)
Electron Transport and Oxidative Phosphorylation
(c)
Fatty Acid Oxidation
(d)
All of above
(e)
None
Ans.: (d) All of above

Q.3
ATP Synthetics or F0/F1 is present on:

(a)
Mitochondrial Matrix
(b)
Inner Mitochondrial Membrane
(c)
Outer Mitochondrial Membrane
(d)
b&c
Ans.: (b)
Q.4
Which of the following is polecat inhibitor of ATP synthesize?

(a)
Kanamycin
(b)
Streptimycin
(c)
a&b
(d)
Oligomycin
Ans.: (d)
Q.5
Oligomycin
Which pair represents isozymes?

(a)
Hexokinase & Fructokinase

78
(b)
Fructokinase & Glucokinase
(c)
Glucokinase & hexokinase
(e)
None
Ans.: (a)
All
Q.6
All
Glycolysis is also known as:

(a)
Lori cycle
(b)
EMP Pathway
(c)
Both
(d)
None
Ans.: (b)
Q.7
(d)
EMP Pathway
Following are the phases of Glycolysis:

(a)
Preparatory Phase
(b)
Pay off phase
(c)
Both
(d)
None
Ans.: (c)
Both
Q.8
Glycolysis occurs in:

(a)
Cytoplasm
(b)
Mitochondria
(c)
Nucleus
(e)
None
Ans.: (a)
Q.9
Cytoplasm
Kreb Cycle is also known as:

(a)
Citric Acid Cycle
(b)
Acetyl Co A catabolism
(c)
Both
(d)
None
Ans.: (c)
Both
Q.10 Succinate dehydrogenase enzyme is found in:

(a)
(b)
(c)
Ans.: (b)
Mitochondrial Matrix
Outer Mitochondrial Membrane
(d)
None
Biochemistry-I
79
Q.11 How many ATP molecules formed during complete oxidation of one mole of
acetyl CoA:
(a)
12
Ans.: (a)
12
(b)
30
(c)
15
(d)
None
Q.12 Carbon dioxide is produced during:

(a) glycolysis
(b) the Kreb's cycle
(c) the mitochondrial electron transport chain
(d) substrate level phosphorylation reactions
(e) all of the reactions above produce carbon dioxide
Ans.: (b) the Kreb's cycle
Q.13 The electron transport chain in the mitochondrion pumps protons from the
________ to the ________.
(a) matrix; intermembrane space
(b) matrix; stroma
(c) intermembrane space; matrix
(d) matrix; cytoplasm
Ans.: (a) matrix; intermembrane space
Q. 14 Given the general equation for respiration, C6 H12*O6 + 6O2 6CO2 + 6 H2O,
which of the following is true?
(a) glucose is reduced to water
(b) oxygen is reduced to carbon dioxide
(c) glucose is oxidized to carbon dioxide
(d) oxygen is oxidized to water
(e) glucose and oxygen are both oxidized to carbon dioxide
Ans.: (c) glucose is oxidized to carbon dioxide
Q.15 The first biochemical pathway to evolve in living things was most likely:
(a) fermentation
(b) glycolysis
(c) the Kreb's cycle
(d) the mitochondrial electron transport chain
Ans.: (b) glycolysis
Q.16 Which of the following statements about glycolysis is TRUE?
(a) no ATP are made during glycolysis
(b) Glycolysis requires 32 ATP to work
(c) One redox reaction occurs during glycolysis
(d) Glycolysis occurs only under anaerobic conditions
80
(e)There are two oxidative phosphorylation reactions during glycolysis

Ans.: (b) Glycolysis requires 32 ATP to work
Q.17 Give an account on EMP Pathway?
Ans.: Glycolysis also called as Embden Mayer Hoff Pathway is an oxidative process in
which one mole of glucose is partially oxidized into 2 moles of Pyruvate. This
Pathway occurs in cytosol of cell.
Overall Reaction:
Glucose + 2NAD+ + 2ADP + 2H2PO4 2Pyruvate +

2NADH + 2ATP + 2H2O
Glycolysis consists of two phases:

(a)
Preparatory Phase: Consist of 5 steps. In these reactions Glucose is

enzymatically phosphorylated by ATP to yield Fructose 1, 6- diphosphate.
(b)
Pay off Phase: The last 5 reactions of Glycolysis constitute this phase in
which energy liberated during conversion of 3 moles of glyceraldehydes- 3
phosphate to 2 moles of pyruvate by coupled phosphorylation of 4 moles of
ADP to ATP. Although 4 moles of ATP are formed in phase II the net overall
yield is only 2 moles of ATP per mole of glucose, since 2 moles of ATP are
invested in phase I. The Phase II is thus energy conserving.
Biochemistry-I
81
Q.18 Give an account of Krebs cycle and explain role of Mitochondria in it?
Ans.: Mitochondria are double membrane bound mobile as well as plastic organelles.
Outer membrane is smooth but inner membrane is highly convoluted; forming
folds called cristae and is highly impermeable to small ions due to having very
high content of phospholipids cardiolipin. Mitochondrial matrix and inner
membrane contain enzymes for Kreb cycle.
82
INNER MEMBRANE
outer membrane
Cristae
MATRIX SPACE
Citric acid cycle was discovered by H. A. Kreb & received Nobel Prize in 1953.
This cycle occurs in matrix of mitochondria (cytosol in prokaryotes). Citric acid
cycle is also known as Tri carboxylic acid cycle. Glycolysis has an aerobic and an
anaerobic nature, the citric acid cycle is strictly aerobic in nature. The main
purpose of citric acid cycle is the conversion of potential chemical energy into
metabolic energy in form of ATP
Energy yield of citric acid cycle:
Reaction
Method of ATP Formation
ATP yield
per mole
Isocitrate Ketogutarate +
Co2
Respiratory chain oxidation of

NADH
Ketogutarate Succinate Co
A + Co2
-do-
Reaction
Method of ATP Formation
ATP yield
per mole
Succinate Co A + ADP + Pi Oxidation at substrate level

Succinate ATP
Succinate Fumarate

FADH2
Malate Oxaloacetate

NADH
Total gain of ATP
12
Biochemistry-I
83
Q. 19 Give structure and function of ATP Synthetase.

Ans.: Mitochondrial inner membrane contains the ATP Synthesizing enzyme complex
called ATP Synthetase or F0 F1 ATP ase. This enzyme complex has 2 major
components F0 & F1. The F1 Component is protruding into matrix from the inner
membrane. It is attached by a stalk to F0 component which is embedded in inner
membrane and extends across it. F1 contains three subunit that are sites of ATP
synthesis. Proton translocation through F0 powers rotation of subunit of F1
leading to changes in conformation of F1 subunits. By means of this binding
change mechanism, the F0 F1 complex harness the proton motive force to power
ATP Synthesis.
84
Section-D
Chapter-1
Chloroplast:
Capturing Energy from Sun
Q.1
Who found that water is an essential requirement for photosynthesis?

(a)
Saussure
(b)
Priestley
(c)
Neil
(d)
None of the above
Biochemistry-I
Ans.: (a)
Q.2
85
Saussure
Photo system I and II are?

(a)
900, 680
(b)
700, 680
(c)
680, 900
(e)
680, 700
Ans.: (b)
700, 680
Q.3
Which metal ion is associated with chlorophyll?

(a)
Mn+2
(b)
Mo
(c)
Fe+2
(d)
Mg+2
Ans.: (d)
Mg+2
Q. 4 The colors of light that are most effective for photosynthesis are
(a) red, blue, and violet
(b) green, yellow, and orange
(c) infrared and ultraviolet
(d) All colors of light are equally effective
Ans.: (a) red, blue, and violet
Q.5 A photosystem consists of
(a) a group of chlorophyll molecules, all of which contribute excited electrons to the
synthesis of ATP.
(b) a pair of chlorophyll a molecules.
(c) a group of chlorophyll molecules held together by proteins.
(d) a group of chlorophyll molecules that funnels light energy toward a single
chlorophyll b molecule.
Ans.: (c) a group of chlorophyll molecules held together by proteins.
Q. 6 Which photosystem is believed to have evolved first?
(a) photosystem I
(b) photosystem II
(c) cyclic photophosphorylation
(d) All photosystems evolved at the same time, but in different organisms.
Ans.: (c) cyclic photophosphorylation
Q.7 The final product of the Calvin cycle is
(a) RuBP
(b) G3P.
86
(c) glucose.
(d) PGA.
Ans.: (b) G3P
Q.8 The part of the cell that traps sunlight to make sugar is the _____
(a) Mitochondria
(b) Chloroplast
(c) nucleus
(d) cytoplasm
Ans.: (b) Chloroplast
Q.9 The chloroplast has stacks of _____ called _____.
(a) thylakoids, grana
(b) grana, thylakoids
(c) ) grana, chlorophyll
(d) ) chlorophyll, grana
Ans.: (a) thylakoids, grana
Q.10 What are the products of photosynthesis?
(A) water and carbon dioxide
(B) water and oxygen
(C) oxygen and carbohydrate
(D) carbohydrate and water
(E) NAD and glucose
Ans.: (C) oxygen and carbohydrate
Q.11 Define Photosynthesis?
Ans.: Photosynthesis is the process by which organisms convert light energy into
chemical energy in the form of reducing power (as NADPH) and ATP and use
these chemicals to drive carbon dioxide fixation and reduction to produce sugars.
Q.12 Write the names of stages of Photosynthesis.
Ans.: (1)
(2)
Light Reactions: cyclic and non cyclic photophosphorylation

Calvin Cycle
Q.13 Write the site for Photosynthesis.

Ans.: Chloroplast in mesophyll cells of leaves.
Biochemistry-I
87
Q.14 Define Quantum Yield?

Ans.: The number of oxygen molecules produced per photon absorbed is called
quantum yield.
Q.15 Light reactions occur in?
(a)
Stroma
(b)
Grana
(c)
Stroma & Grana
(c)
None of above
Ans.: (b)
Grana
Q.16 Calvin cycle occur in?

(a)
Grana
(b)
Stroma
(c)
Both
(d)
None of above
Ans.: (b)
Stroma
88
Q.17 Give a brief account on Role of chloroplast Or Function of chloroplast?

Ans.: Chloroplast capture energy form sunlight and use it to fix carbon by process
called photosynthesis. Many reactions that occur in chloroplast during
photosynthesis are grouped into two categories.
(a)
In light reactions energy derived from sunlight energized electron in green

pigment chlorophyll, electron moves in electron transport chain in
thylakoid membrane. Chlorophyll obtain electrons form water, producing
O2 as by product. During electron transport process H+ is pumped across
thylakoid membrane and resulting electro chemical gradient drives ATP
synthesis in stroma. In final step high energy electron are loaded together
with H+ on to NADP+, conversion it into NADPH, all these reactions are
confine to chloroplast.
(b)
In carbon fixation reactions ATP and NADPH produced by Electron

transfer reactions serve as source of energy & reducing power to drive
conversion of CO2 to carbohydrate. Carbon fixation reactions occur in
cytosol of chloroplast produce sucrose and other organic molecules in
leaves which is exported to other tissues as source of organic molecules
and energy.
Q.18 Describe the structure and organization of chloroplasts?

Ans.: Chloroplast is most prominent members of plastid family of organelles found in
all living plant cells. They have permeable outer membrane and less permeable
inner membrane. The space between them is called inter membrane space. Inner
membrane surrounds large space called stroma. Chloroplast has its own genome
and genetic system and stroma therefore contains special set of ribosome, RNA
and chloroplast DNA.
A district membrane that form disc like sacs called thylakoids. Thylakoid
membrane contains electron transport chains, ATP synthases. Thylakoid
membrane is separated form stroma by thylakoid space.
Thylakoids in chloroplast contain pigment require for capturing solar energy
called chlorophyll. It gives green color to leaves and absorbs light in violet &
blue, red regions in between 400 nm -700 nm.
Chlorophyll is large molecule composed of four 5 member rings called Pyrole
rings and central core of magnesium. It also contain side chain called phytol
chain, chlorophyll a is major pigment involved in trapping & converting light
energy into chemical energy. Chlorophyll molecules act as reaction centers.
Carotenoids are also present in thylokoid membrane are called accessory
Biochemistry-I
89
pigments /antenna complexes; harvest light from different wavelengths of

spectrum other then of chlorophyll.
The accessory pigments and reaction centre together form Photo system. Photo
system I constitutes chl a with maximum absorbtion at 700 nm & Photo system II,
chl a with peak absorbtion at 680 nm, act as reaction centre.
Q.19 What is Light Reaction? Explain.
Ans.: Light driven reactions of Photosynthesis are called light. It is initiated by
absorbtion of light by P680 (PS II). P680 get excited, transfer electron to acceptor
molecule. P680 becomes strong oxidizing agent split water to release oxygen. This
light dependent splitting of water molecules is called photolysis Mn+2, Ca+2, Cl
are also required for photolysis ,due to break down of water electrons are passed
to P680 which is able to restore the electrons from water molecules. From P680
electron is accepted by primary electron acceptor which gets reduced & donates
electron to other downstream components of electron transport chain.
Photo system I is exited on absorbing light and get oxidized. It transfer its
electron to primary electron acceptor while transfer electron to Ferrodoxin NADP reductase to reduce NADP+ to NADPH. NADPH is then used in reduction
of Co2 to Carbohydrates in carbon fixation reaction. This reaction requires energy
in form of ATP produced from ADP in presence of light called
Photophosphorylation.
Q.20 Describe cyclic and non cyclic photo phosphorylation?
Ans.: (a) Non-cyclic photo phosphorylation: Is a result of an interaction of Photo
system I and PS II. There is Continuous flow of electrons from water to PS II to PS
I & finally to NADP, as electron pass downhill, ATP is formed from ADP because
the electron flow from water to INADP is unidirectional. This process of ATP
formation is called non-cyclic Photo phosphorylation.
(b) Cyclic photo phosphorylation: Yield only ATP and produce no net change in
oxidation & reduction state of any electron donor or acceptor. The pathway
begins when PS I complex absorb solar energy. High energy electrons leave PS I
reaction centre chl a molecule but eventually return to it.
90
Non cyclic photophosphorylation
Ridox Potential (ev)
Electron acceptor
ADP + Pl
Cyt b6
ATP
2e
Cyt f
Biochemistry-I
91
Reaction Centre (P700)

Antenrro Molecules
PS I
Light
Cyclic Photo phosphorylation
Q.21 Explain Calvin cycle?

Ans.: It is also known as Biosynthetic phase or Calvin Benson cycle is a series of
biochemical reactions taking place in stroma of chloroplast of Eukaryotic
photosynthetic organisms ATP and NADPH formed during Light Reaction are
utilized for assimilation of Co2 to Carbohydrates. It is also known as C3 pathway
because the first stable compound forms is 3 Carbon molecules called 3
phosphoglycerate. Plant which fix Co2 using C3 path way called C3 plants.
The reaction of this cycle is loaded into 3 phases.
(1) Carbon Fixations
(2)
Reductions
(3)
Regenerations
92
CALVIN CYCLE
Q.22 Explain C4 pathway? Give examples of C4 plants.
Ans.: It is CO2 concentrating mechanism Phosphoenol pyruvate (PEP) is carboxylated
to C4 acids which are first product of photosynthesis. C4 acids are formed in
mesophyll and diffused to bundle sheath where they are decarboxylated. Buddle
sheath contain Rubisco of Calvin cycle results in formation of C 3 compound
which returns to mesophyll. Examples of C4 plants are maize, sugar cane etc.
C4 plants possess two types of photosynthetic cell layer surrounding vascular

bundle called bundle sheaths which are thick walled & suberized and are not
Biochemistry-I
93
directly connected to inter cellular spaces of mesophyll. Mesophyll cells are

connected to bundle sheath by large numbers of plasmodesmata.
Q.23 what do you mean by CAM pathway? Explain.
Ans.: Crassulacean acid Metabolism (CAM) refer to a mechanism of photosynthesis
that is different form C3 & C4 pathway. Occurs only in succulents and plants that
grow in dry conditions e. g.; Cactus, pineapple etc. In CAM plants, CO2 is taken
up by leaves on green stems through stomata which remain open in night, during
day stomata remain closed in these plants to conserve moisture. CO2 taken up in
night is fixed to form malic acid which is stored in vacuole. Malice acid formed
during night is used during day as a source of CO2 for photosynthesis to proceed
through C3 pathway.
This pathway is a kind of an adaptation which allows carrying out
photosynthesis without loss of water.
94
Chapter-2
Enzymes
Q.1
who coined the term Enzyme?

(a)
Louise Pasteur
(b)
Sumner
(c)
Kuhne
(d)
None of the above
Ans.: (c)
Kuhne
Q.2
Who is known as Father of Modern Enzymologist?

(a)
Buchner
(b)
Khune
(c)
Northrop and Kunity
(d)
Sumner
Ans.: (d)
Q.3
Sumner
Write names of two model gain to explain formation of Enzyme-Substrate

Complex?
Ans.: (a)
Fischers Lock and key Model.
(b)
Koshlands Induced Fit Model.
Q.4
Match the Following:

Vitamin
Coenzyme/Cofactors
(a) Thiamine
(1) Pyruvate Kinase
(b) Fe+2 or Fe+3
(2) Coenzyme A
(c) Riboflavin
(3) Carbonic anhydrase
(d) K+
(4) FAD and FMN
(e) Pantothenic Acid
(5) cytochrome Oxidase, Catalase
(f) Zn+2
(6) Thiamine Pyrophosphate
(I)
(a) (6), (b) (5), (c) (4), (d) (1), (e) (2), (f) (3)
(II)
(a) (6), (b) (4), (c) (1), (d) (5), (e) (3), (f) (2)
(III)
(a) (6), (b) (2), (c) (3), (d) (1), (e) (5), (f) (4)
Biochemistry-I
(IV)
Ans.: (I)
Q.5
95
None of these
(a) (6), (b) (5), (c) (4), (d) (1), (e) (2), (f) (3)
Which of the following is true for specific constants.

Kcat x Km, affinity
(c)
Kcat
Measure enzyme efficiency (d) none of the above
Km
Ans.: (c)
(b)
Km
, enzyme concentration
Kcat
(a)
Kcat
measure enzyme efficiency
Km
Q.6 Which of the following does NOT apply to an enzyme.

(a) Catalyst
(b) Inorganic
(c) Protein
(d) All of the above apply to an enzyme
Ans.: (b) Inorganic
Q.7 The non protein part of an enzyme is known as
(a) Holoenzyme
(b) Apoenzyme
(c) Prosthetic group
(d) Vitamins
Ans.: (c) Prosthetic group
Q.8 The polypeptide or protein part of the enzyme called
(a) Holoenzyme
(b) Apoenzyme
(c) Prosthetic group
(d) Zymogen
Ans.: (b) Apoenzyme
Q.9 Turn over number of an enzyme is dependent upon
(a) Size of enzyme
(b) Molecular weight of enzyme
(c) Active sites
(d) Concentration of substrate
Ans.: (c) Active sites
96
Q.10 Coenzymes combine with

(A) Proenzymes
(B) Apoenzymes
(C) Holoenzymes
(D) Antienzymes
Ans.: (B) Apoenzymes
Q.11 Write the chemical nature of Enzymes?

Ans.: Proteinaceous
Q.12 Define Enzymes?
Ans.: Enzymes are catalyst (Biocatalyst) that changes the rate of reaction without being
changed themselves. Enzymes are highly specific and their activity can be
regulated.
Q.13 Differentiate between Endo & Exo enzymes?
Ans.: Enzymes that usually act within the cells in which they are produced are called
Endo enzymes whereas, certain enzymes which are liberated by living cells,
catalyze useful reactions outside cell in its environment are called Exo enzymes.
Q.14 What are Simple and Conjugated Enzymes?
Or
Give a brief account of Coenzymes/Cofactors.
Ans.: Simple Protein Enzymes: are completely protein e.g. amylase, papain etc. Complex
Protein Enzymes: are composed of a protein portion called the apoenzyme and one or
more nonprotein portions. There are two main categories of such substances:
Cofactors are inorganic metal ions such as iron, magnesium or zinc.
Coenzymes are organic compounds composed of vitamins or vitamin derivatives.
Examples include NAD+, NADP+ and FAD+, all of which serve in the transfer of electrons
and hydrogens released by catabolic pathways.
Both cofactors and coenzymes help to complete the structure of a conjugated

enzyme, forming a holoenzyme.
Biochemistry-I
97
Q.15 What are General characteristics of Enzymes.

Ans.: (1)
Enzymes are Colloidal in nature.
(2)
Enzymes exhibit enormous catalytic Power.
(3)
They are specific in action.
(4)
Enzymes are heat sensitive.
(5)
They are capable of bringing about reversion in chemical reaction.
(6)
pH value also controls the activity to great extent.
Q.16 Define the following?

(a)
Active Site
(b)
Transition State
(c)
Activation Energy.
Ans.: (a)
Active site: active site of an enzyme is the region often a cleft or crevice on
surface of enzyme that binds the substrate and converts it into product. It
is usually a small part of whole enzyme and is a three dimensional entity
formed by amino acid residues.
(b)
Transition State : At top of energy hill is a point at which decay to S or P

state is equally probable is called transition state and is different from
reaction inter mediate.
98
(c)
Activation Energy: The difference between the energy levels of ground

state and transition state is called Gibbs free energy of activation or simple
activation energy.
Q.17 Give the free energy diagram for chemical reaction, S P

Ans.:
Transition State (T*)
Energy coordinate
(Free Energy, G)
GS
S(Ground State)
3
GP
P(Ground State)
G
Reaction Coordinate
Where
S
Free energy of Substrate
Free energy of Product
Activation energies for the two reactions; S P & P S
Overall standard free energy change in moving Trans to P
Q.18 What is Turn over Number?

Ans.: The number of substrate molecules converted into product per unit time when
enzyme is fully saturated with substrate is called Turn over Number.
Q.19 What are Isoenzymes?
Ans.: Many enzymes occur in more than one molecular form in same tissue or ever in
same cell in such cases the different forms of enzymes catalyze some reaction but
Biochemistry-I
99
they possess different kinetic properties and different amino acid composition,
These multiple forms of enzymes are called Isoenzymes or Isozymes.
Examples; Lactic dehydrogenase (LDH) which exists in 5 possible forms in
various organs of most vertebrates.
Reaction; Lactic + NAD+ Pyruvate + NADH + H+
LDH
Following are the different types of LDH found;
(a)
Heart LDH: 4 identical subunits called H subunits active at low level of

Pyruvate.
(b)
Muscle LDH: 4 identical subunits called M subunits and is active at high

concentrations of Pyruvate.
Combination of H and M subunits produce 3 additional types of hybrid enzymes

& 5 possible forms e. g. H4, H3M, H2M2, HM3, M4 server concentration of LDH is
often used in diagnosis of myocardial infarction.
Other noteworthy, examples of Isoenzymes are MDH (malic dehydrogenase)
hexokinase etc.
Q.20 Give a brief account on Nomenclature of enzymes.
Ans.: Nomenclature of enzymes is based on the following points:
(a)
Substrate acted upon by enzyme: enzymes have been named by adding

suffix ase in the name of substrate catalyzed e. g. Lipases, Sucrose.
(b)
Type of reaction catalyzed: e.g. hydrolyses (Catalyses hydrolysis),

oxidizes (oxidation) etc.
(c)
Substrate acted upon & type of reaction catalyzed: e.g. Succinate

dehydrogenase catalyze dehydrogenation of substrate succinic acid.
(d)
Substance that is synthesized: e. g. Fumarase that forms fumarate

irreversibly form L malate.
(e)
Chemical Composition of enzymes :
(f)
(1)
Pepsin Consisting protein only.
(2)
Carbonic anhydrase containing protein and anhydrase cation.
(3)
Pyruvate oxidase Containing protein and organic compound

(Flavo proteins)
Substance hydrolyzed and group involved :

(1)
Carbohydrate hydrolyzing enzymes; Glycosidases cellulose.

100
(2)
Protein hydrolyzing enzymes : Endo peptidases Pepsin, trypsin

Endopeptidases dipeptidases, tripeptidases.
(3)
Lipid hydrolyzing lipases, esterases.
Q.21 What is Michaelis Menten hypothesis. Derive Michaelis Menten equation?

Ans.: Michaelis and Menten while studying hydrolysis of sucrose catalyzed by enzyme
invertase proposed Michaelis Menten hypothesis on the basis of following
assumptions.
(1)
Only single substrate and a single product are involved.
(2)
Process provides essentially to completion.
(3)
Concentrating of substrate is much greater than that of enzyme in system.
(4)
An intermediate enzyme substrate complex is formed.
They postulates that the enzyme (E) forms a weakly bonded complex (ES) with
substrate (S) (ES) on hydrolysis yield product and free enzyme (E).
Reaction : E + S
ES E + P
Following; symbol may be used for deriving Michelis Menten equation:

(Et)
Total Concentration of enzyme.
(S)
Total Concentration of substrate
(ES)
Concentration of Enzyme Substrate complex.
(Et) (ES)
Concentration of free enzyme.
Now,
Rate of appearance of products (is velocity: V) is proportional to concentration of
the enzyme substrate complex
V = K (ES)
_ _ _ _ (1)
Maximum reaction rate Vm will occur at a point when total enzyme E t is bound to
substrate. Then maximum concentration of ES will be equal to total enzyme
concentration Et
Vm = K (Et)
_ _ _ _ (2)
Dividing eq n (1) by (2)

V (ES)
=
Vm (E t )
_ _ _ _ (3)
Biochemistry-I
101
For, reversible reaction, E + S E S equilibrium constant for dissociation of ES as

km is equal tv
Km =
(E t ) - (ES) (S)
(ES)
_ _ _ _ (4)
(ES) x Km = (Et) x (S) (ES) x (S)

Or
(ES) x Km + (ES) x (S) = (Et) x (S)
Or
(ES)
(S)
=
(E t ) Km + (S)
Substituting the value of
_ _ _ _ (5)
((ES)
form eq. (3) to eq. (5) ;
(E t )
V
(S)
=
Vm Km + (S)
_ _ _ _ (6)
Or
V=
Or
Vm x (S)
Km + (S)
Km = (S)
_ _ _ _ (7)
Vm 1
V
_ _ _ _ (8)
equations (7) is called Michaelis Menten equation and the equilibrium constant
Km is called Michaelis constant is a measure of affinity of an enzyme for its
substrate.
Q.22 Write short note on classification of enzymes.
Ans.: The International Union of Biochemistry (IUB) instituted a Systemic Scheme for
enzyme. Each enzyme is now classified and named according to type of chemical
reaction it catalyzes:
(1)
Oxidoreductases: Catalyze oxidation

dehydrogenase, oxidase reductases etc.
reduction
(2)
Transferases: Catalyze reaction that involves transfer of groups from one

molecule to another e. g.; amino, carboxyl etc.
(3)
Hydrolyses: Catalyze reactions in which change bonds is accomplished by

adding water e.g.; esterase, peptidases.
(4)
Lyses : Catalyze reactions in which group H2O, CO2, NH3 are remove to
form double bond or are added to double bond e.g.; Decarboxylases,
Synthases.
reactions
e.g.;
102
(5)
Isomerases: Catalyze intra molecular rearrangements and yield isomeric

forms. The epimerases Catalyze inversion of asymmetric carbon atom,
mutases Catalyze intra molecular transfer of functional group.
(6)
Ligases: Formation of C C, C S, C O & C N bonds and energy of these

reactions is supplied by ATP hydrolysis e.g.; Synthetase, Carboxylases.
Q.23 Give an account of Allosteric regulation of enzymes?

Or
What is feed back inhibition? What are allosteric enzymes?
Ans.: In biological systems the rates of many enzymes are altered by presence of other
molecules such as activators and inhibitors collectively called as effectors.
A, common regulation of metabolic pathway is when an enzyme early in the
pathway is inhibited by end-product of metabolic pathway in which it is involved
called feed back inhibition. End product of metabolic pathway involving
multiple enzyme reactions, it will bind to enzyme at control point at a site other
than active sites: Such enzymes are called Allosteric enzymes.
Allosteric enzymes give Sigmoid Curve rather then hyperbolic plots predicted by
Michaelis Menten equation.
Allosteric enzymes are made up of two or more sub units. Enzymes for which
substrate and effector are same called homotropic and enzymes for which
effectors and substrate are different called heterotropic.
Example of Allosteric enzyme: Aspartate transcarbamoylase used in Pyrimidine
biosynthesis.
Biochemistry-I
103
Chapter-3
Vitamins
Q.1 Milk is deficient in which vitamins?
(A)Vitamin C
(B) Vitamin A
(C) Vitamin B2
(D) Vitamin K
Ans.: (A) Vitamin C
Q.2 Vitamin B12:
(A) is fat-soluble
(B) requires a glycoprotein from absorption
(C) contains a haeme ring
(D) is water soluble
Ans.: Both b and c
Q. 3 Which one of these vitamins has a role as an antioxidant?

(A) Biotin
(B) Folate
(C) Niacin
(D) Pantothenic acid
(E) Vitamin E
Ans.: (E) Vitamin E
Q.4 Deficiency of which one of these vitamins is a major cause of blindness?
(A) Vitamin A
(B) Vitamin B12
(C) Vitamin B6
(D) Vitamin D
(E) Vitamin K
Ans.: (A) Vitamin A
104
Q.5 Which of the following vitamins is essential for fatty acid synthesis?
(A) Folate
(B) Pantothenic acid
(C) Vitamin B6
(D) Vitamin B12
(E) Vitamin C
Ans.: (B) Pantothenic acid
Q.6 Which one of these vitamins is involved in blood clotting?
(A) Vitamin B6
(B) Vitamin B12
(C) Vitamin D
(D) Vitamin E
(E) Vitamin K
Ans.: (E) Vitamin K
Q.7 Which of the following vitamins provides the cofactor for pyruvate dehydrogenase?
(A) Folate
(B) Niacin
(C) Riboflavin
(D) Thiamin
(E) Vitamin B6
Ans.: (D) Thiamin
Q.8 Which one of these vitamins has a role in oxidation and reduction reactions?
(A)Folate
(B)Niacin
(C)Pantothenic acid
(D)Vitamin A
(E)Vitamin B6
Ans. (B)Niacin
Q.9 Which one of these vitamins is required for DNA synthesis?

(A) Biotin
(B) Folate
(C) Pantothenic acid
(D) Vitamin B6
(E) Vitamin B12
Ans.: (B) Folate
Q.10 Deficiency of which one of these vitamins may lead to haemolytic anaemia?
(A) Vitamin B6
(B) Vitamin B12
Biochemistry-I
105
(C) Vitamin D
(D) Vitamin E
(E) Vitamin K
Ans.: (D) Vitamin E
Q.1
Who introduced the term VITAMINE?
Ans.: Funk with Dr. Max Nierenstein.

Q.2
Who gives alphabetical nomenclature of vitamins?
Ans.: Sir J. C. Drummond.

Q.3
Define vitamins.
Ans.: According to Franz Holfmeister vitamins are substances which are indispensable
for growth and maintenance of animal organism, which occur both in animals
and plants and are present in small amounts in food.
Or
Vitamins refer to substances distinct form major compounds of food, required in
minute quantities and their absence causes specific deficiency.
Q.4
Give a brief idea about general characteristics of vitamins.
Ans.: (1)
Widespread occurrence in nature both in plant and animal worlds.
(2)
All common food stuffs contain more than one vitamin.
(3)
The plants can synthesize all vitamins where as only a few vitamins are
synthesized in animals.
(4)
Human body can synthesize same vitamins e.g.; Vit. A, B, C, D.
(5)
Most vitamins have been artificially synthesized.
(6)
All the cells of body store vitamins to some extent.
(7)
Vitamins are partly destroyed and are partly excreted.
(8)
Vitamins are non-antigenic.
(9)
Vitamins carry out functions in very low concentrations and their daily
requirement is very low.
(10)
Vitamins are effective when taken orally.
(11)
Need of vitamins increases with the increasing age.

106
(12)
Q.5
Synthetically made vitamins are just as nutritionally good as natural

vitamins.
How Vitamins are classified and comment on the storage of vitamins in Body?
Ans.: Two categories of vitamins are usually recognized.

(a)
Fat soluble vitamins.
(b)
Water soluble vitamins.
Fat soluble Vitamins:

(1)
Not really soluble in water.
(2)
Contain C, H, O e.g. are Vitamins A, D, E, K.
(3)
Are isoprenoid compouds.
(4)
Fat soluble vitamins are stored in liver.
(5)
Are building blocks of many naturally occurring oily, greasy or rubbery

substances of plant origin
(6)
Although Fat soluble vitamins are storable but increase in their uptake can
result in toxic conditions (also called as hyper vitaminoses)
(b) Water soluble Vitamins
Q. 6
(1)
Besides C, H, O contain (N).
(2)
Are catalytic factors and they having very vital role to play in biochemical
reactions characteristic of all living objects.
(3)
B, C: [choline, inositol, p-amino benzoic acid befavanoeds, -lipoic acid are

also frequently included in this category. But some do not considered them
as true vitamins.
(4)
Stored in lesser amounts in cell vit. C is stored in adrenal cortex.
Give a brief account of Fat soluble Vitamins covering following pointsproperty and their Role.
Ans.: Vitamins A, D, E, K is Fat soluble vitamins.

(I)
VITAMIN A
First isolated form fish liver at by Holmes.
Liver oils of various fishes are richest natural sources of vitamin A.
Biochemistry-I
107
It is supplied by all pigmented (yellow) vegetables and fruits such as carrots,

pumpkins, yellow corn, tomatoes etc.
Absent in vegetable fats and oils.
Structure: Found in two forms A1 and A2
Corticoids
Vitamins A
(Pro-vitamin A)
, ,
Carotenes come under carotenoids.
Vitamin A1 is primary alcohol called retinol (C2 OH29 OH) contain
-ionone
ring.
Vitamin A2 contain additional conjugate double bond between carbon atoms
3 & 4 of
ionone rings, also called as 3-dehydorretinol
Properties: oxidizing agents.
Relatively less stable in air unless protected by vitamin E.
Role and Metabolism:
Carotene (From Plants)
Retinal
Retinoic acid
Retinol
Retinylester
Absorbed through lymphatic system

& stored in Liver
Liver can also convert retinol to retinoic acid which is also, quickly absorbed
from the intestine.
Vitamin A maintains Skins epithelial cells and lining of digestive,
respiratory and genitourinary system.
Guards against cancer by producing cell wall from undesirable oxidation &
scavenging the products of oxidation.
Deficiency disease:
(1) Xeropthalmia (blindness in childhood)
(2) Keratomalacia (corneal disease)
108
(3) Phrynoderma : Skin lesion

(II)
VITAMIN D
Two forms Vitamin D2 and D3 are more important.
Vitamin D is present in its pro vitamin form in human skin and is easily
converted to active form by irradiation with ultraviolet light.
Best source are Liver oils of fishes, egg yolks.
Absent in vegetable fats and oils.
Structure:
(1)
Ergosterol Inter Mediates Ergocalciferol or Viosterol (Vitamin D2)
(2)
7-dehydrocholestrol Cholecalciferol (Vitamin D3)
Biologically active form of Vitamin D3 is: 25 hydro cholesterol more polar and
has an additional OH group at C 25. It is synthesized in liver and is converted to
1, 25 dihydroxy cholecalciferol in kidneys.
Properties: (1) Soluble in fat and fat solvents.
(2) White and crystalline substance.
(3) Resistant to oxidation and not affected by acids and alkalis.
Vitamin D has important role in calcification of bones and teeth by inverse
absorbtion of Ca+2 and phosphate salts.
Pro vitamins D3 can be synthesized within human body that and therefore
not required in diet.
Increased need of this vitamin is required in growth and during pregnancy.
Deficiency Diseases:
Rickets: No Calcification of bones.
Osteomalacia: Softening of bones, C/P ratio gets disturbed.
(III)
VITAMIN E
Also called as anti fertility factor.
Were isolated from wheat germ oil by Evans (found in tow form
tocopherol) in wheat germ oil.
and
Biochemistry-I
109
Plant oils such as wheat germ, rice, corn, soybean & meat, milk, egg etc are
also source of Vitamin E.
Widely spread forms of vitamin E are , ,
tocopherols.
Structure: The other name for Vitamin E is Tochopherols which is a lipid

molecule.
A various tocopherols differ form each other in substitutes on carbon 5, 7
and 8.
Compositon of variable segment of different Tocopherols.
Types of Tocopherol
Substituents of carbon atoms

5
Alfa
CH3
CH3
CH3
Beta
CH3
CH3
CH3
CH3
Gamma
Properties:
(1)
Vitamin E is resistant to heat and acids.
2)
Are antioxidants.
(3)
Vitamin E can be destroyed by UV rays.
(4)
It is found in the non specifiable fraction of the vegetable oils.

(1)
Duet to its antioxidizing property, it is commercially added to food to retard

their spoilage.
(2)
Tocopherols protect mitochondrial system from inactivation by fat

peroxides.
(3)
Catabolism of
- tocopherol involves both the oxidative cleavage of
chromon ring to yield quinine or hydroquinone like compounds and
degradation of isprenoids side chain.
Deficiency Disease:
(1) Development of sterility in rats.
(2) Muscular Dystrophy in herbivores like rabbits and guniea pigs.
(III)
VITAMIN K
110
(1)
Also called as antihemorragic factor or Coagulation vitamin.
(2)
Two naturally occurring forms of vitamin K are vitamin K1 and vitamin K2.
(3)
Vitamin K1 occurs in green vegetables like spinach, alfalfa, cabbage and

Vitamin K2 found in intestinal bacteria and putrefied fish meal.
Structure:
(1)
Vitamin K1 and K2 are the derivatives of quinones.
(2)
These two forms differ in the composition of the side chain present at carbon
3 of napthoquinone ring.
(3)
Vitamin K1 (C31 H46 O2) has side chain of phytol radical whereas vitamin K2
(C41 H56 O2) has Difarnesyl radical as a side chain.
(4)
Common analogues of napthoquinones possessing vitamin K activity are

menadione (K3) and phthiocol.
Properties:
(1)
Vitamin K1 is yellow visual oil & Vitamin K2 is yellowish crystalline solid.
(2)
It can be destroyed by irradiations strong acids, alkalis & oxidizing agents.
(3)
It is light sensitive and therefore kept in dark bottles.

(1)
It is fat soluble and absorbed in presence of bile.
(2)
Vitamin K has essential role in prothrombin biosynthesis needed in process

of blood clotting & produced in liver.
(3)
It is also required in Electron

Phosphorylation in Mitochondria.
transport
system
and
Deficiency Disease:
(1) Hemorrhage due to loss of blood clotting.
(2) Steatorrhea Diminished intestinal absorbtion of lipids.
Coenzyme Q
(1)
Components of Mitochondrial lipids.
(2)
Coenzyme Q serves as electron transport of agent
(3)
Contain 6 to 10 isoprene unit.
Stigma sterol
(1)
Fat soluble vitamin.
(2)
It is plant sterol isolated from soybean and wheat germ oils.

oxidative
Biochemistry-I
(3)
Q.7
111
Also called as anti stiffness factor.
Write short note on Vitamin B Complex.
Ans.: At present Vitamin B Complex is known to consist of group of at least 13

components usually named as B1, B2, and B3 etc.
Vitamin B1: Also called as Thiamine and commonly known as anti beriberi factor
found in all plant and animal food. Thiamine is 2, 5 diethyl 6 amino pyrimidine
bonded to 4 methyl hydroxyethyl thiozole through methylene linkage.
Thiamine is while crystalline Substance, readily soluble in water destroyed at
elevated temperature but it is stable in acidic medium.
It is present mainly as its coenzyme (TPP) which participates in decarboxylation
of - Keto acids and in Trans ketolation. It deficiency causes Berry Berry:
Vitamin B2: Also known as Riboflavin or Lactoflavin or yellow enzyme. Found in
Milk, cheese, eggs Riboflavin (CH H2O N4 O6) belongs to water soluble pigments
called lyochromes. Thiamine molecule consists of sugar alcohol D ribitol attached
to iso alloxazinc ring. Riboflavin is bright orange yellow crystalline powder stable
to heat and acid but decomposed by alkalis & light. Riboflavin is phosphorlated
and converted to FMN (flavin mono nucleotide) which is essential in biosynthesis
of fats. They play key role in cell metabolism & function in accepting hydrogen
atom form reduced pyridine nucleotides person deficient in vitamin B2 show
chelosis (fissuring at corners of mouth), Glossitis, smooth tongue and loss of
papillary structure occurs.
Vitamin B3 (Pantothenic acid): Also known as filtrate or yeast factor. The
coenzyme form of this vitamin is Coenzyme A or CoA- SH found in Vegetables
like potatoes, cabbage, fruits like peanuts etc. Pantothenic acid is an amide of
pantoic acid and - alanine. It is pale yellow viscous oil stable in oxidizing,
reducing agent and destroyed by acidic and alkaline medium Vitamin B3
participate information of biologically important Co A and function as Thioester
of Carboxylic acids. Deficiency of vitamin B3 causes de pigmentation of skin,
hairs, atrophy of adrenal cortex in animals like rat.
Vitamin B5: Also known as pellagra preventive factor (PP) factor. Chemically it is
called Nicotinic acid, most abundantly found in yeast, Liver, Pork, red meat are
good sources of vitamin B5.
Niacin or vitamin B5 is pyridine derivative and its amide is known as
Nicotinamide. The conversion of niacin to niacin amide takes place in kidney. The
112
niacin in Man is derived from amino acid tryptophan. The two forms (Coenzyme
forms) of vitamin NAD and NADP carry out Reduction of flavin coenzymes and
oxidation of alcohols, aldehydes, amino acids. Deficiency of niacin causes pellagra
in man and black tongue in dogs.
Vitamin B6: This group includes three compounds Pyridoxine, Pyridoxal,
Pyridoxamine. Also called as anti dermatitis factor, cereals, peas, sweet potatoes,
egg yolk, fish, beaf and cows milk are rich source of vitamin B6. It is derivative of
pyridoxine. Pyridoxine is white crystalline substance and is sensitive to light and
UV radiation.
The three forms of vitamin B6 are converted to pyridoxal phosphate which act as
coenzyme in various enzymatic reactions involved in amino acid metabolism
such as transamination decarboxylation, racemization and in metabolism of
glycogen and fatty acids. Deficiency results dermatitis anemia.
Vitamin B7: Also known as Biotin. Yeast, liver, kidney, milk are among richest
source of vitamin B7. Usually it occurs in bonded form called Biocytin. Biotin
consists of fused imidazole and thiophene ring with fatty acid side chain.
Biotin crystallizes as long needles. It is heat stable and resistant to acids and
alkalis. This vitamin is Coenzyme for enzyme catalyzing CO2 fixation in organic
molecules. Deficiency results in dermatitis, decrease is weight, hair loss etc.
Vitamin B9: Commonly called as Liver Lactobacillus casei factor. It is found in
salmon, dates, spinach root vegetables etc. Chemically it is also called as folic acid
consists of 3 units: glutamic acid, -amino benzoic acid and derivative of hetero
cyclic fused ring compound. It is yellow Crystalline Substance, stable to heat, in
alkaline or neutral conditions reduced from DHFA is dihydrofolic acid or FH 2 act
as coenzymes associated with oxidation of NADPH to NADP Vitamin B9 group is
also involved in one carbon metabolism. Deficiency diseases are anemia in chicks,
in man leads to megaloblastic anemia, glossitis etc.
Vitamin B12: Commonly called as anti pernicious anemia factor (APA) and
chemically is known as Cyanocobalamin, chief sources are milk, meat, eggs, fish.
It has tetrapyrrole ring structure with co atom in its trivalent state.
Vitamin B12 Coenzyme is 5 deoxyadinosyl Cobalamine, It is the only known
Coenzyme with carbon metal bond in a bio-molecule.
Biochemistry-I
113
Coenzyme B12 serves as carrier of methyl group to appropriate acceptor, it is

associated with isomerisation of dicarboxylic acid. It also affects myelin
formation. Deficiency diseases include juvenile pernicious anemia, adult
pernicious anemia.
Q.8
Write short note on Vitamin C?
Ans.: It is commonly called as ascorbate; citrus fruits (like orange and lemon) are good
sources of vitamin C. Not synthesized by primates. It is derivative of hexose
called L-gulose. Chemically it is also known as ascorbic acid.
It is colorless, odorless, crystalline substance. Ascorbic acid function in many
activities e.g.; formation tissue collagen, Vitamin C help in conversion of folic
acid to tetra hydrofolic acid and also play important role in tyrosine metabolism.
A vitaminosis C leads to scurvey or bleeding gums, anemia, delayed wound
healing, tender bones, edematous swellings etc.
Q.9
What are Choline and inositol?
Ans.: Choline is also included in vitamins. The riches sources are egg yolk, liver, meats,
cereals, vegetables like beans, peanuts. It is important constituent of lecithin.
It is quaternary ammonium compound and is water soluble. It undergoes
esterification with acetyl CoA to form acetyl choline which is a Neurotransmitter,
deficiency leads to haemorrhages in kidneys, fatty livers in rates.
Ionositol: Found in muscle, liver, kidney, brain and tissues of eye. In plants it
occurs in fruits, vegetables. It occurs in four forms; ionositol, phytin, phophatidyl
inositol and nondialzyable complex ionositol.
Ionositol is Corboxylic hexahydric alcohol, Myoinositol found in muscles is
biologically active. It is sweet in taste and soluble in water. It is essential for
transport processes in cells.
Deficiency results in retarted growth however its deficiency does not occur in
man.
114
Biochemistry-I
115
B.Sc. /M.Sc. (Part I) Examination, 2011

(Faculty of Science)
(Common to Three and Five Year Integrated Course)
BIOTECHNOLOGY
Paper BT- 302
BIOCHEMISTRY-I
Year-2011
Time Allowed: 3 Hours
Max. Marks: 50
Attempt five questions in all, including Question No.1 which is compulsory, selecting ONE
question from each Section.
1. Answer the following questions in short:(i) What is the major constituent of living beings?
(ii)
What functions do Lysosomes play in the cell?
(iii)
Define Co-factors and Coenzymes.
(iv)
What is Chargaffs law?
(v)
Who discovered repetitive DNA?
(vi)
Who are CAM plants?
(vii)
How much angel is formed between two bonds in a structure of water molecule?
(viii)
How much angle is formed between two O-H bonds in a structure of water
molecule?
(ix)
What is the difference between nucleoside and nucleotide?
(x)
What are Vitamins?
1 x 10 =10
Section-A
2. Describe the structure, chemical organization and functions of plasma membrane.
3+4+3=10
3. Write notes on:
(i) Bacterial and Plant Cell Walls.
116
(ii) Golgi bodies.

(iii)Endoplasmic reticulum.
4+3+3=10
Section-B
4. Explain the biological significance of water.
10
5. Write an essay on Bio-molecules.
10
Section-C
6. What is mitochondria? Give an illustrated account of reactions and importance of Krebs
cycle.
3+5+2=10
7. Write notes on:

(a) Structure and function of various part of nucleus.
(b) DNA Replication
5+5=10
Section-D
8. What are chloroplasts? Explain light and dark reactions of photosynthesis.

3+7=10
9. Write Classification of enzymes and explain reaction and derivation of Michaelis-Menten
equation kinetics.
5+5=10
*****************
Biochemistry-I
117
Key Terms
A form. A duplex DNA structure with right-handed twisting in which the planes of the base pairs
are tilted about 70 with respect to the helix axis.
Acetal. The product formed by the successive condensation of two alcohols with a single
aldehyde. It contains two ether-linked oxygens attached to a central carbon atom.
Acetyl CoA. Acetyl-coenzyme A, a high-energy ester of acetic acid that is important both in the
tricarboxylic acid cycle and in fatty acid biosynthesis. Active site. The region of an enzyme
molecule that contains the substrate binding site and the catalytic site for converting the
substrate(s) into product(s).
Active transport. The energy-dependent transport of a substance across a membrane.
Adenine. A purine base found in DNA or RNA.
Adenosine. A purine nucleoside found in DNA, RNA, and many cofactors.
Adenosine diphosphate (ADP). The nucleotide formed by adding a pyrophosphate group to the
5'-OH group of adenosine.
Adenosine triphosphate (ATP). The nucleotide formed by adding yet another phosphate group
to the pyrophosphate group on ADP.
Adenylate cyclase. The enzyme that catalyzes the formation of cyclic 3',5' adenosine
monophosphate (cAMP) from ATP.
Adipocyte. A specialized cell that functions as a storage depot for lipid.
Aerobe. An organism that utilizes oxygen for growth.
Affinity chromatography. A column chromatographic technique that employs attached
functional groups that have a specific affinity for sites on particular proteins.
Alcohol. A molecule with a hydroxyl group attached to a carbon atom.
Aldehyde. A molecule containing a doubly bonded oxygen and a hydrogen attached to the same
carbon atom.
Alleles. Alternative forms of a gene.
118
Allosteric enzyme. An enzyme whose active site can be altered by the binding of a small
molecule at a nonoverlapping site.
Angstrom (). A unit of length equal to 10-10 m.
Anomers. The sugar isomers that differ in configuration about the carbonyl carbon atom. This
carbon atom is called the anomeric carbon atom of the sugar.
Antibiotic. A natural product that inhibits bacterial growth (is bacteriostatic) and sometimes
results in bacterial death (is bacteriocidal).
Antibody. A specific protein that interacts with a foreign substance (antigen) in a specific way.
Anticodon. A sequence of three bases on the transfer RNA that pair with the bases in the
corresponding codon on th messenger RNA.
Antigen. A foreign substance that triggers antibody formation and is bound by the corresponding
antibody.
Antiparallel b-pleated sheet (b-sheet). A hydrogen bonded secondary structure formed between
two or more extended polypeptide chains.
Autoradiography. The technique of exposing film in the presence of disintegrating radioactive
particles. Used to obtain information on the distribution of radioactivity in a gel or a thin cell
section.
B form. The most common form of duplex DNA, containing a right-handed helix and about 10
(10.5 exactly) base pairs per turn of the helix axis.
Beta-bend (b-bend) or turn. A characteristic way of turning an extended polypeptide chain in a
different direction, involving the minimum number of residues, and held together by hydrogen
bonding.
Beta-sheet (b-sheet). A sheetlike structure formed by the interaction between two or more
extended polypeptide chains.
Beta-oxidation (b-oxidation). Oxidative degradation of fatty acids that occurs by the successive
oxidation of the b-carbon atom.
Base. The adenine, guanine, cytosine or thymine group attached to a nucleotide or nucleoside.
Also may be used to refer to a nucleic acid unit within a polynucleotide chain, as when a gene is
said to be 2000 bases long.
Base analog. A compound, usually a purine or a pyrimidine, that differs somewhat from a normal
nucleic acid base.
Biochemistry-I
119
Base stacking. The close packing of the planes of base pairs, commonly found in DNA and RNA
structures.
Bidirectional replication. Replication in both directions away from the origin, as opposed to
replication in one direction only (unidirectional replication).
Bilayer. A double layer of lipid molecules with the hydrophilic ends oriented outward, in contact
with water, and the hydrophobic parts oriented inward.
Bile salts. Derivatives of cholesterol with detergent properties that aid in the solubilization of
lipid molecules in the digestive tract.
Biochemical pathway. A series of enzyme-catalyzed reactions that results in the conversion of a
precursor molecule into a product molecule.
Biomolecule : A biomolecule is any molecule that is produced by a living organism, including
large macromolecules such as proteins, polysaccharides, lipids, and nucleic acids.
Bond energy. The energy required to break a bond.
Buffer. A conjugate acid-base pair that is capable of resisting changes in pH when acid or base is
added to the system. This tendency will be maximal when the conjugate forms are present in
equal amounts.
cAMP. 3',5' cyclic adenosine monophosphate. The cAMP molecule plays a key role in metabolic
regulation
Carbohydrate. A polyhydroxy aldehyde or ketone.
Carboxylic acid. A molecule containing a carbon atom attached to a hydroxyl group and to an
oxygen atom by a double bond.
Carcinogen. A chemical that can cause cancer.
Carotenoids. Lipid-soluble pigments that are made from isoprene units.
Catabolism. That part of metabolism that is concerned with degradation reactions.
Catabolite repression. The general repression of transcription of genes associated with
catabolism that is seen in the presence of glucose.
Catalyst. A compound that lowers the activation energy of a reaction without itself being
consumed.
Catalytic site. The site of an enzyme involved in the catalytic process.
120
cDNA. Complementary DNA, made in vitro from the mRNA by the enzyme reverse transcriptase
using deoxyribonucleotide triphosphates. Unlike mRNA, cDNA can be easily propagated and
sequenced.
Cell commitment. That stage in a cell's life when it be comes committed to a certain line of
development.
Cell cycle. All of those stages that a cell passes through from one cell generation to the next.
Cell line. An established clone originally derived from a whole organism through a long process
of cultivation.
Cell lineage. The pedigree of cells resulting from binary fission.
Cell wall. A tough outer coating found in many plant, fungal, and bacterial cells that accounts for
their ability to withstand mechanical stress or abrupt changes in osmotic pressure. Cell walls
always contain a carbohydrate component and frequently also a peptide and a lipid component.
Chelate. A molecule that contains more than one binding site and frequently binds to another
molecule through more than one binding site at the same time.
Chlorophyll. A green photosynthetic pigment that is made of a magnesium dihydroporphyrin
complex.
Chloroplast. A chlorophyll-containing photosynthetic organelle, found in eukaryotic cells, that
can harness light energy.
Chromatin. The nucleoprotein fibers of eukaryotic chromosomes.
Chromatography. A procedure for separating chemically similar molecules. Segregation is
usually carried out on paper or in glass or metal columns with the help of different solvents. The
paper or glass columns contain porous solids with functional groups that have limited affinities
for the molecules being separated.
Chromosome. A thread-like structure, visible in the cell nucleus during metaphase, that carries
the hereditary information.
Chromosome puff. A swollen region of a giant chromosome; the swelling reflects a high degree
of transcription activity.
Cis dominance. Property of a sequence or a gene that exerts a dominant effect on a gene to which
it is linked.
Cistron. A genetic unit that encodes a single polypeptide chain.
Biochemistry-I
121
Citric acid cycle. See tricarboxylic acid (TCA) cycle.

Coactivator. A molecule that functions together with a protein apoactivator. For example, cAMP
is a coactivator of the CAP protein.
Codon. In a messenger RNA molecule, a sequence of three bases that represents a particular
amino acid.
Coenzyme. An organic molecule that associates with enzymes and affects their activity.
Cofactor. A small molecule required for enzyme activity. It could be organic in nature, like a
coenzyme, or inorganic in nature, like a metallic cation.
Complementary base sequence. For a given sequence of nucleic acids, the nucleic acids that are
related to them by the rules of base pairing.
Configuration. The spatial arrangement in which atoms are covalently linked in a molecule.
Conformation. The three-dimensional arrangement adopted by a molecule, usually a complex
macromolecule. Molecules with the same configuration can have more than one conformation.
Consensus sequence. In nucleic acids, the "average" sequence that signals a certain type of
action by a specific protein. The sequences actually observed usually vary around this average.
Cytidine. A pyrimidine nucleoside found in DNA and RNA.
Cytochromes. Heme-containing proteins that function as electron carriers in oxidative
phosphorylation and photosynthesis.
Cytokinin. A plant hormone produced in root tissue.
Cytoplasm. The contents enclosed by the plasma (or cytoplasmic) membrane, excluding the
nucleus.
Cytosine. A pyrimidine base found in DNA and RNA.
Cytosol. The liquid portion of the cytoplasm, including the macromolecules but not including the
larger structures like subcellular organelles or cytoskeleton.
D loop. An extended loop of single-stranded DNA displaced from a duplex structure by an
oligonucleotide.
Dalton. A unit of mass equivalent to the mass of a hydrogen atom (1.66 x 10-24 g)
122
Dark reactions. Reactions that can occur in the dark, in a process that is usually associated with
light, such as the dark reactions of photosynthesis.
De novo pathway. A biochemical pathway that starts from elementary substrates and ends in the
synthesis of a biochemical.
Deamination. The enzymatic removal of an amine group, as in the deamination of an amino acid
to an alpha keto acid.
Dehydrogenase. An enzyme that catalyzes the removal of a pair of electrons (and usually one or
two protons) from a substrate molecule.
Denaturation. The disruption of the native folded structure of a nucleic acid or protein molecule;
may be due to heat, chemical treatment, or change in pH.
Density-gradient centrifugation. The separation, by centrifugation, of molecules according to
their density, in a gradient varying in solute concentration.
Dialysis. Removal of small molecules from a macromolecule preparation by allowing them to
pass across a semipermeable membrane.
Diauxic growth. Biphasic growth on a mixture of two carbon sources in which one carbon source
is used up before the other one. For example, in the presence of glucose and lactose, E. coli will
utilize the glucose before the lactose.
Difference spectra. Plots comparing the absorption spectra of a molecule or an assembly of
molecules in different states, for example, those of mitochondria under oxidizing or reducing
conditions.
Differential centrifugation. Separation of molecules and/or organelles by sedimentation rate.
Differentiation. A change in the form and pattern of a cell and the genes it expresses as a result
of growth and replication, usually during development of a multicellular organism. Also occurs in
microorganisms (e.g. in sporulation).
Dimer. Structure resulting from the association of two subunits.
Diploid cell. A cell that contains two chromosomes (2N) of each type.
Dipole. A separation of charge within a single molecule.
Disulfide bridge. A covalent linkage formed by oxidation between two cysteine SH groups either
in the same polypeptide chain or in different polypeptide chains. Reversible by adding reducing
agents.
Biochemistry-I
123
DNA. Deoxyribonucleic acid. A polydeoxyribonucleotide in which the sugar is deoxyribose; the

main repository of genetic information in all cells and most viruses.
DNA cloning. The propagation of individual segments of DNA as clones.
DNA library. A mixture of clones, each containing a cloning vector and a segment of DNA from
a source of interest.
DNA polymerase. An enzyme that catalyzes the formation of 3'-5' phosphodiester bonds from
deoxyribonucleotide triphosphates.
Domain. A segment of a folded protein structure showing conformational integrity. A domain
could include the entire protein or just a fraction of the protein. Some proteins, such as antibodies,
contain many structural domains.
Dominant. Describing an allele whose phenotype is expressed regardless of whether the
organism is homozygous or heterozygous for that allele.
Double helix. A structure in which two helically-twisted polynucleotide strands are held together
by hydrogen bonding and base stacking.
Duplex. Same as double helix.
Electrophoresis. The movement of particles in an electrical field. A commonly-used technique
for analysis of mixtures of molecules in solution according to their electrophoretic mobilities.
Elongation factors. Protein factors uniquely required during the elongation phase of protein
synthesis. Elongation factor G (EF-G) brings about the movement of the peptidyl tRNA from the
A site to the P site of the ribosome.
Eluate. The fluid that has passed through (eluted from) a chromatographic column.
Endergonic reaction. A reaction with a positive standard free energy change.
End-product (feedback) inhibition. The inhibition of the first enzyme in a pathway by the end
product of that pathway.
Endocrine glands. Specialized tissues whose function is to synthesize and secrete hormones.
Endonuclease. An enzyme that breaks a phosphodiester linkage at some point within a
polynucleotide chain.
Endopeptidase. An enzyme that breaks a polypeptide chain at an internal peptide linkage.
124
Endoplasmic reticulum. A system of double membranes in the cytoplasm that is involved in the
synthesis of transported proteins. The rough endoplasmic reticulum has ribosomes associated
with it. The smooth endoplasmic reticulum does not.
Energy charge. The fractional degree to which the AMP-ADP-ATP system is filled with highenergy phosphates (phosphoryl groups).
Enhancer. A DNA sequence that can stimulate transcription at an appreciable distance from the
site where it is located. It acts in either orientation and either upstream or downstream from the
promoter.
Entropy. The randomness of a system.
Enzyme. A moleucle, most often a protein, that contains a catalytic site for a biochemical
reaction.
Epimers. Two stereoisomers with more than one chiral center that differ in configuration at one
of their chiral centers.
Equilibrium. The point at which the concentrations of two compounds are such that the
interconversion of one compound into the other compound does not result in any change in free
energy.
Escherichia coli (E. coli). A Gram negative bacterium commonly found in the vertebrate
intestine. It is the bacterium most frequently used in the study of biochemistry and genetics.
Eukaryote. A cell or organism that has a membrane-bound nucleus.
Excision repair. DNA repair in which a damaged region is replaced.
Excited state. An energy-rich state of an atom or a molecule, produced by the absorption of
radiant energy.
Exergonic reaction. A chemical reaction that takes place with a negative change in standard free
energy.
Exon. A segment within a gene that carries part of the coding information for a protein.
Exonuclease. An enzyme that breaks a phosphodiester linkage at one or the other end of a
polynucleotide chain so as to release single or small nucleotide residues.
Facultative aerobe. An organism that can use molecular oxygen in its metabolism but that also
can live anaerobically.
Biochemistry-I
125
Fatty acid. A long-chain hydrocarbon containing a carboxyl group at one end. Saturated fatty
acids have completely saturated hydrocarbon chains. Unsaturated fatty acids have one or more
carbon-carbon double bonds in their hydrocarbon chains.
Feedback inhibition. See end-product inhibition.
Fermentation. The energy-generating breakdown of glucose or related molecules by a process
that does not require molecular oxygen.
Fingerprinting. The characteristic two-dimensional paper chromatogram obtained from the
partial hydrolysis of a protein or a nucleic acid.
Fluorescence. The emission of light by an excited molecule in the process of making the
transition from the excited state to the ground state.
Frameshift mutations. Insertions or deletions of genetic material that lead to a shift in the
translation of the reading frame. The mutation usually leads to nonfunctional proteins.
Free energy. That part of the energy of a system that is available to do useful work.
G1 phase. That period of the cell cycle in which preparations are being made for chromosome
duplication, which takes place in the S phase.
G2 phase. That period of the cell cycle between S phase and mitosis (M phase).
Gametes. The ova and the sperm, haploid cells that unite during fertilization to generate a diploid
zygote.
Gel fitration chromatography. A technique that makes use of certain polymers that can form
porous beads with varying pore sizes. In columns made from such beads, it is possible to separate
molecules, which cannot penetrate beads of a given pore size, from small molecules that can.
Also called gel-exclusion or molecular seive chromatography.
Gene. A segment of the genome that codes for a functional product.
Gene amplification. The duplication of a particular gene within a chromosome two or more
times.
Gene splicing. The cutting and rejoining of DNA sequences.
General recombination. Recombination that occurs between homologous chromosomes at
homologous sites.
Generation time. The time it takes for a cell to double its mass under specified conditions.
126
Genetic map. The arrangement of genes or other identifiable sequences on a chromosome.

Genome. The total genetic content of a cell or a virus.
Genotype. The genetic characteristics of an organism (distinguished from its observable
characteristics, or phenotype).
Globular protein. A folded protein that adopts an approximately globular shape. May also be
called soluble proteins.
Gluconeogenesis. The production of sugars from nonsugar precursors such as lactate or amino
acids. Applies more specifically to the production of free glucose by vertebrate livers.
Glycogen. A polymer of glucose residues in 1,4 linkage, with 1,6 linkages at branchpoints.
Glycogenic. Describing amino acids whose metabolism may lead to gluconeogenesis.
Glycolipid. A lipid containing a carbohydrate group.
Glycolysis. The catabolic conversion of glucose to pyruvate with the production of ATP.
Glycoprotein. A protein linked to an oligosaccharide or a polysaccharide. Glycosaminoglycans.
Long, unbranched polysaccharide chains composed of repeating disaccharide subunits in which
one of the two sugars is either N-acetylglucosamine or N-acetylgalactosamine.
Glycosidic bond. The bond between a sugar and an alcohol. Also the bond that links two sugars
in disaccharides, oligosaccharides, and polysaccharides.
Glyoxylate cycle. A pathway that uses some of the enzymes of the TCA cycle and some enzymes
whereby acetate can be converted into succinate and carbohydrates.
Glyoxysome. An organelle containing some enzymes of the glyoxylate cycle
Golgi apparatus. A complex series of double-membrane structures that interact with the
endoplasmic reticulum and that serve as a transfer point for proteins destined for other organelles,
the plasma membrane, or extracellular transport.
Gram molecular weight. For a given compound, the weight in grams that is numerically equal to
its molecular weight.
Ground state. The lowest electronic energy state of an atom or a molecule.
Growth factor. A substance that must be present in the growth medium to permit eucaryotic cell
proliferation.
Biochemistry-I
127
Growth fork. The region on a DNA duplex molecule where synthesis is taking place. It
resembles a fork in shape, since it consists of a region of duplex DNA connected to a region of
unwound single strands.
Guanine. A purine base found in DNA or RNA.
Guanosine. A purine nucleoside found in DNA and RNA.
Hairpin loop. A single-stranded complementary region of DNA or RNA that folds back on itself
and base-pairs into a double helix.
Half-life. The time required for the disappearance of one half of a substance.
Haploid cell. A cell containing only one chromosome of each type.
Heavy isotopes. Forms of atoms that contain greater numbers of neutrons than the most common
form (e.g., 15N, l3C).
Helix. A spiral structure with a repeating pattern.
Heme. An iron-porphyrin complex found in hemoglobin and cytochromes. Hemiacetal. The
product formed by the condensation of an aldehyde with an alcohol; it contains one oxygen linked
to a central carbon in a hydroxyl fashion and one oxygen linked to the same central carbon by an
ether linkage.
Henderson-Hasselbalch equation. An equation that relates the pKa, to the pH and the ratio of
the proton acceptor (A-) and the proton donor (HA) species of a conjugate acid base pair.
Heterochromatin. Highly condensed regions of chromosomes that are not usually
transcriptionally active.
Heteroduplex. An annealed duplex structure between two DNA strands that do not show perfect
complementarity. Can arise by mutation, recombination, or the annealing of complementary
single-stranded DNAs.
Heteropolymer. A polymer containing more than one type of monomeric unit.
Heterotroph. An organism that requires preformed organic compounds for growth.
Heterozygous. Describing an organism (a heterozygote) that carries two different alleles for a
given gene.
Hexose. A sugar with a six-carbon backbone.
128
High-energy compound. A compound that undergoes hydrolysis with a high negative standard
free energy change.
Histones. The family of basic proteins that is normally associated with DNA in most cells of
eukaryotic organisms.
Holoenzyme. An intact enzyme containing all of its subunits and any necessary cofactors with
full enzymatic activity.
Homologous chromosomes. Chromosomes that carry the same pattern of genes, but not
necessarily the same alleles.
Homopolymer. A polymer composed of only one type of monomeric building block.
Homozygous. Describing an organism (a homozygote) that carries two identical alleles for a
given gene.
Hormone. A chemical substance made in one cell and secreted so as to influence the metabolic
activity of a select group of cells located at other sites in the organism.
Hormone receptor. A protein that is located on the cell membrane or inside the responsive cell
and that interacts specifically with the hormone.
Host cell. A cell used for growth and reproduction of a virus.
Hybrid (or chimeric) plasmid. A plasmid that contains DNA from two different organisms.
Hydrogen bond. A weak, noncovalent, attractive force between one electronegative atom and a
hydrogen atom that is covalently linked to a second electronegative atom.
Hydrolysis. The cleavage of a molecule by the addition of water. Hydrophilic. Preferring to be in
contact with water.
Hydrophobic. Preferring not to be in contact with water, as is the case with the hydrocarbon
portion of a fatty acid or phospholipid chain.
Hydrophobic effect. The noncovalent association of nonpolar groups with each other in aqueous
solution.
Hydroxyapatite. A calcium phosphate gel used, in the case of nucleic acids, to selectively absorb
duplex DNA-RNA from a mixture of single-stranded and duplex nucleic acids.
Icosahedral symmetry. The symmetry displayed by a regular polyhedron that is composed of 20
equilateral triangular faces with 12 corners.
Biochemistry-I
129
Imine. A molecule containing a nitrogen atom attached to a carbon atom by a double bond. The
nitrogen is also covalently linked to a hydrogen. Immunofluorescence. A cytological technique in
which a specific fluorescent antibody is used to label an antigen. Frequently used to determine the
location of an antigen in a tissue or a cell.
Immunoglobulin. A protein made in a B plasma cell and usually secreted; it interacts specifically
with a foreign agent. Synonymous with antibody. It is composed of two heavy and two light
chains linked by disulfide bonds. Immunoglobulins can be divided into five classes (IgG, IgM,
IgA, IgD, and IgE) based on their heavy-chain component.
Inducible proteins. Those which are synthesized in different amounts depending on cellular
signals.
In vitro. Literally, "in glass," describing whatever happens in a test tube or other receptacle, as
opposed to what happens in whole cells of the whole organism (in vivo).
Induced fit. A change in the shape of an enzyme that results from the binding of substrate.
Inducers. Molecules that cause an increase in a protein activity when added to cells.
Initiation factors. Those protein factors that are specifically required during the initiation phase
of protein synthesis.
Intron. A segment of the nascent transcript that is removed by splicing. Also refers to the
corresponding region in the DNA. Synonymous with intervening sequence.
Inverted repeat. A chromosome segment that is identical to another segment on the same
chromosome except that it is oriented in the opposite direction.
Ion-exchange resin. A polymeric resinous substance, usually in bead form, that contains fixed
groups with positive or negative charge. An anion exchange resin has positively-charged groups
and is therefore useful in exchanging the anionic groups in a test sample; a cation exchange resin
is itself negatively charged, and has the opposite application. The resin is usually used in a
column chromatographic procedure.
Isoelectric point or pH. The pH at which a protein has no net charge.
Isomerase. An enzyme that catalyzes an intramolecular rearrangement.
Isomerization. Rearrangement of atomic groups within the same molecule without any loss or
gain of atoms.
Isozymes. Multiple forms of an enzyme that differ from one another in one or more of the
properties.
130
Ketone. A functional group of an organic compound in which a carbon atom is double-bonded to

an oxygen. Neither of the other substituents attached to the carbon is a hydrogen. Otherwise the
group would be called an aldehyde.
Ketone bodies. Refers to acetoacetate, acetone, and b-hydroxybutyrate made from acetyl-CoA in
the liver and used for energy in nonhepatic tissue.
Ketosis. A condition in which the concentration of ketone bodies in the blood or urine is
unusually high.
Kilobase. One thousand bases in a DNA molecule.
Kinase. An enzyme catalyzing phosphorylation of an acceptor molecule, usually with ATP
serving as the phosphate (phosphoryl) donor.
Law of mass action. The finding that the rate of a chemical reaction is a function of the product
of the concentrations of the reacting species.
Leader region. The region of an mRNA between the 5' end and the initiation codon for
translation of the first polypeptide chain.
Leader sequence. An N-terminal signal sequence that directs secretion and processing of
proteins.
Lectins. Agglutinating proteins usually extracted from plants.
Ligand. A (usually small) molecule that binds to another, such as oxygen when it binds to
myoglobin.
Ligase. An enzyme that catalyzes the joining of two molecules together. In DNA it joins 5'-OH to
3' phosphates.
Lipid. A biological molecule that is soluble in organic solvents. Lipids include steroids, fatty
acids, prostaglandins, terpenes, and waxes.
Lipid bilayer. Model for the structure of the cell membrane based on the interaction between the
hydrophobic regions of phospholipids.
Lipopolysaccharide. Usually refers to a unique glycolipid found in Gram negative bacteria.
Lyase. An enzyme that catalyzes the removal of a group to form a double bond, or the reverse
reaction.
Lysosome. An organelle that contains hydrolytic enzymes designed to break down proteins that
are targeted to that organelle.
Biochemistry-I
131
Lytic infection. A virus infection that leads to the Iysis of the host cell, yielding progeny virus
particles.
Membrane. A sheet-like composite of protein and lipid that is the boundary of cells and
organelles.
Membrane protein. A protein that is associated with a membrane, rather than found free in the
cell. A membrane protein may be integral (embedded or buried) in the membrane, or peripheral
(attached more loosely, by interactions with either lipid or intergral membrane proteins).
Membrane transport. The facilitated transport of a molecule across a membrane.
Merodiploid. An organism that is diploid for some but not all of its genes.
Mesosome. An invagination of the bacterial cell membrane.
Messenger RNA (mRNA). The template RNA carrying the message for protein synthesis.
Metabolic turnover. A measure of the rate at which already existing molecules of the given
species are replaced by newly-synthesized molecules of the same type. Usually isotopic labeling
is required to measure turnover.
Metabolism. The sum total of the enzyme-catalyzed reactions that occur in a living organism.
Metamorphosis. A change of form, especially the conversion of a larval form to an adult form.
Metaphase. That stage in mitosis or meiosis when all of the chromosomes are lined up on the
equator (i.e., an imaginary line that bisects the cell).
Micelle. An aggregate of lipids in which the polar head groups face outward and the hydrophobic
tails face inward; no solvent is trapped in the center.
Michaelis constant (Km). The substrate concentration at which an enzyme-catalyzed reaction
proceeds at one-half of the maximum velocity.
Michaelis-Menten equation (also known as the Henri-Michaelis-Menten equation). An equation
relating the reaction velocity to the substrate concentration of an enzyme.
Microtubules. Thin tubules, made from globular proteins, that serve multiple purposes in
eukaryotic cells.
Mismatch repair. The replacement of a base in a heteroduplex structure by one that forms a
Watson-Crick base pair.
132
Missense mutation. A change in which a codon for one amino acid is replaced by a codon for
another amino acid.
Mitochondrion. An organelle, found in eukaryotic cells, in which oxidative phosphorylation
takes place. It contains its own genome and unique ribosomes to carry out protein syn thesis of
only a fraction of the proteins located in this organelle.
Nascent RNA. The initial transcripts of RNA, before any modification or processing.
Negative control. Repression of biological activity by the presence of a specific molecule.
Nernst equation. An equation that relates the redox potential to the standard redox potential and
the concentrations of the oxidized and reduced form of the couple.
Nuclease. An enzyme that cleaves phosphodiester bonds of nucleic acids.
Nucleic acids. Polymers of the ribonucleotides or deoxyribonucleotides.
Nucleohistone. A complex of DNA and histone.
Nucleolus. A spherical structure visible in the nucleus during interphase. The nucleolus is
associated with a site on the chromosome that is involved in ribosomal RNA synthesis.
Nucleophilic group. An electron-rich group that tends to attack an electron-deficient nucleus.
Nucleosome. A complex of DNA and an octamer of histone proteins in which a small stretch of
the duplex is wrapped around a molecular bead of histone.
Nucleoside. An organic molecule containing a purine or pyrimidine base and a five-carbon sugar
(ribose or deoxyribose).
Nucleotide. An organic molecule containing a purine or pyrimidine base, a five-carbon sugar
(ribose or deoxyribose), and one or more phosphate groups. A phosphoester of a nucleoside.
Nucleus. In eukaryotic cells, the centrally-located organelle that encloses most of the
chromosomes. Minor amounts of chromosomal substance are found in some other organelles,
most notably the mitochondria and the chloroplasts.
Okazaki fragment. A short segment of single-stranded DNA that is an intermediate in DNA
synthesis. In bacteria, Okazaki fragments are 1000-2000 bases in length; in eukaryotes, 100-200
bases in length.
Oligonucleotide. A polynucleotide containing a small number of nucleotides. The linkages are
the same as in a polynucleotide; the only distinguishing feature is the small size.
Biochemistry-I
133
Oligosaccharide. A molecule containing a small number of sugar residues joined in a linear or a

branched structure by glycosidic bonds.
Oncogene. A gene of cellular or viral origin that is responsible for rapid, unruly growth of animal
cells. A cancer-causing gene.
Operon. A group of contiguous genes that are coordinately regulated by two cis-acting elements,
a promoter and an operator. Found only in prokaryotic cells.
Optical activity. The property of a molecule that leads to rotation of the plane of polarization of
plane-polarized light when the latter is transmitted through the substance. Chirality is a necessary
and sufficient property for optical activity.
Organelle. A subcellular membrane-bounded body with a well-defined function.
Osmotic pressure. The pressure generated by the mass flow of water to that side of a membranebounded structure that contains the higher concentration of solute molecules. A stable osmotic
pressure is seen in systems in which the membrane is not permeable to some of the solute
molecules.
Oxidation. The loss of electrons from a compound.
Oxidative phosphorylation. The formation of ATP as the result of the transfer of electrons to
oxygen.
Oxido-reductase. An enzyme that catalyzes oxidation-reduction reactions.
Palindrome. A sequence of bases that reads the same in both directions on opposite strands of the
DNA duplex (e.g., GAATTC).
PCR. Polymerase chain reaction. A method for amplifying DNA sequences.
Pentose. A sugar with five carbon atoms.
Pentose phosphate pathway. The pathway involving the oxidation of glucose-6-phosphate to
pentose phosphates and further reactions of pentose phosphates.
Peptide. An organic molecule in which a covalent amide bond is formed between the a-amino
group of one amino acid and the a-carboxyl group of another amino acid, with the elimination of
a water molecule. The resulting connection is called a peptide bond.
Peptide mapping. Same as fingerprinting.
134
Peptidoglycan. The main component of the bacterial cell wall, consisting of a two-dimensional
network of heteropolysaccharides running in one direction, cross-linked with polypeptides
running in the perpendicular direction.
Periplasm. The region between the inner (cytoplasmic) membrane and the cell wall or outer
membrane of a bacterium.
Permeable. The property of allowing material to pass through, as a permeable membrane.
Permease. A protein that catalyzes the transport of a specific small molecule across a membrane.
Peroxisomes. Subcellular organelles that contain flavin-requiring oxidases and that regenerate
oxidized flavin by reaction with oxygen.
Phenotype. The observable trait(s) that result from the genotype in cooperation with the
environment.
Phenylketonuria. A human disease caused by a genetic deficiency in the enzyme that converts
phenylalanine to tyrosine. The immediate cause of the disease is an excess of phenylalanine,
which can be alleviated by a diet low in phenylalanine.
Pheromone. A hormone-like substance that acts as an attractant.
Phosphodiester. A molecule containing two alcohols esterified to a single molecule of
phosphate. For example, the backbone of nucleic acids is connected by 5'-3' phosphodiester
linkages between the adjacent individual nucleotide residues.
Phospholipid. A lipid containing charged hydrophilic phosphate groups; a component of cell
membranes.
Phosphorylation. The formation of a phosphate derivative of a biomolecule.
Photosynthesis. The biosynthesis that directly harnesses the chemical energy resulting from the
absorption of light. Frequently used to refer to the formation of carbohydrates from CO 2 that
occurs in the chloroplasts of plants or the plastids of photosynthetic microorganisms.
Pitch length (or pitch). The number of base pairs per turn of a duplex helix.
Plasma membrane. The membrane that surrounds the cytoplasm.
Polar group. A hydrophilic (water-loving) group.
Polyamine. A hydrocarbon containing more than two amino groups.
Biochemistry-I
135
Polycistronic messenger RNA. In prokaryotes, an RNA that contains two or more cistrons; note
that only in prokaryotic mRNAs can more than one cistron be utilized by the translation system to
generate individual proteins.
Polymerase. An enzyme that catalyzes the synthesis of a polymer from monomers.
Polynucleotide. A chain structure containing nucleotides linked together by phosphodiester (5'3') bonds. The polynucleotide chain has a directional sense with a 5' and a 3' end.
Polynucleotide phosphorylase. An enzyme that polymerizes ribonucleotide diphosphates. No
template is required.
Polypeptide. A linear polymer of amino acids held together by peptide linkages. The polypeptide
has a directional sense, with an amino- and a carboxy-terminal end.
Polyribosome (polysome). A complex of an mRNA and two or more ribosomes actively engaged
in protein synthesis.
Polysaccharide. A linear or branched chain structure containing many sugar molecules linked by
glycosidic bonds.
Porphyrin. A complex planar structure containing four substituted pyrroles covalently joined in a
ring and frequently containing a central metal atom. For example, heme is a porphyrin with a
central iron atom.
Positive control. A system that is turned on by the presence of a regulatory protein.
Post translational modification. The covalent bond changes that occur in a polypeptide chain
after it leaves the ribosome and before it becomes a mature protein.
Primary structure. In a polymer, the sequence of monomers and the covalent bonds. In proteins,
it refers to the amino acid sequence.
Primer. A structure that serves as a growing point for polymerization. Short primers of DNA are
often used in sequencing and mutagenesis procedures.
Primosome. A multiprotein complex that catalyzes synthesis of RNA primer at various points
along the DNA template.
Prokaryote. A unicellular organism that contains a single chromosome, no nucleus, no
membrane-bound organelles, and has characteristic ribosomes and biochemistry.
Promoter. That region of the gene that signals RNA polymerase binding and the initiation of
transcription.
136
Prophase. The stage in meiosis or mitosis when chromosomes condense and become visible as
refractile bodies.
Proprotein. A protein that is made in an active form, so that it requires processing to become
functional.
Prostaglandin. An oxygenated eicosanoid that has a hormonal function. Prostaglandins are
unusual hormones in that they usually have effects only in that region of the organism where they
are synthesized.
Prosthetic group. Synonymous with coenzyme except that a prosthetic group is usually more
firmly attached to the enzyme it serves.
Protein subunit. One of the components or monomers of a multicomponent protein.
Proteoglycan. A protein-linked heteropolysaccharide in which the heteropolysaccharide is
usually the major component.
Protist. A relatively undifferentiated organism that can survive as a single cell.
Proton acceptor. A functional group capable of accepting a proton from a proton donor
molecule.
Proton motive force (Dp). The thermodynamic driving force for proton translocation.
Proto-oncogene. A cellular gene that can undergo modification to a cancer-causing gene
(oncogene).
Purine. A heterocyclic ring structure with varying functional groups. The purines adenine and
guanine are found in both DNA and RNA.
Pyranose. A simple sugar containing the six-membered pyran ring.
Pyrimidine. A heterocyclic six-membered ring structure. Cytosine and uracil are the main
pyrimidines found in RNA, and cytosine and thymine are the main pyrimidines found in DNA.
Pyrophosphate. A molecule formed by two phosphates in anhydride linkage.
Quaternary structure. In a protein, the way in which the different folded subunits interact to
form the multisubunit protein.
R group. Shorthand for the side chain of an amino acid.
R loop. A triple-stranded structure in which RNA displaces a DNA strand by DNA-RNA hybrid
formation in a region of the DNA
Biochemistry-I
137
Recombination. The transfer to offspring of genes not found together in either of the parents.
Redox couple. An electron donor and its corresponding oxidized form.
Redox potential (E). The relative tendency of a pair of molecules to release or accept an
electron. The standard redox potential (E0) is the redox potential of a solution containing the
oxidant and reductant of the couple at standard concentrations.
Regulatory enzyme. An enzyme in which the active site is subject to regulation by factors other
than the enzyme substrate. The enzyme frequently contains a nonoverlapping site for binding the
regulatory factor that affects the activity of the active site.
Regulatory gene. A gene whose principal product is a protein designed to regulate the synthesis
of other genes.
Renaturation. The process of returning a denatured structure to its original native structure, as
when two single strands of DNA are reunited to form a regular duplex, or an unfolded
polypeptide chain is returned to its normal folded three-dimensional structure.
Repair synthesis. DNA synthesis following excision (cutting out) of damaged DNA.
Repetitive DNA. A DNA sequence that is present in many copies per genome.
Replica plating. A technique in which an impression of a culture is taken from a master plate and
transferred to a fresh plate. The impression can be of bacterial clones or phage plaques.
Replication fork. The Y-shaped region of DNA at the site of DNA synthesis; also called a
growth fork.
Replicon. A genetic element that behaves as an autonomous replicating unit. It can be a plasmid,
phage, or bacterial chromosome.
Repressor. A regulatory protein that inhibits transcription from one or more genes. It can
combine with an inducer (resulting in specific enzyme induction) or with an operator element
(resulting in repression).
Resonance hybrid. A molecular structure that is a hybrid of two structures that differ in the
locations of some of the electrons. For example, the benzene ring can be drawn in two ways, with
double bonds in different positions. The actual structure of benzene is in-between these two
equivalent structures.
Restriction-modification system. A pair of enzymes found in most bacteria (but not eukaryotic
cells). The restriction enzyme recognizes a certain sequence in duplex DNA and makes one cut in
each unmodified DNA strand at or near the recognition sequence. The modification enzyme
138
methylates (or modifies) the same sequence, thus protecting it from the action of the restriction
enzyme.
Reverse transcriptase. An enzyme that synthesizes DNA from an RNA template, using
deoxyribonucleotide triphosphates.
Rho factor. A protein involved in the termination of transcription of some messenger RNAs.
Ribose. The five-carbon sugar found in RNA.
Ribosomal RNA (rRNA). The RNA parts of the ribosome.
Ribosomes. Small cellular particles made up of ribosomal RNA and protein. They are the site,
together with mRNA, of protein synthesis.
RNA (ribonucleic acid). A polynucleotide in which the sugar is ribose.
RNA polymerase. An enzyme that catalyzes the formation of RNA from ribonucleotide
triphosphates, using DNA as a template.
RNA splicing. The excision of a segment of RNA, followed by a rejoining of the remaining
fragments.
Rolling circle replication. A mechanism for the replication of circular DNA. A nick in one
strand allows the 3' end to be extended, displacing the strand with the 5' end, which is also
replicated, to generate a double-stranded tail that can become larger than the unit size of the
circular DNA.
Salting in. The increase in solubility that is displayed by typical globular proteins upon the
addition of small amounts of certain salts, such as ammonium sulfate.
Salting out. The decrease in protein solubility that occurs when salts such as ammonium sulfate
are present at high concentrations.
Salvage pathway. A family of reactions that permits, for instance, nucleosides as well as purine
and pyrimidine bases resulting from the partial breakdown of nucleic acids to be re-utilized in
nucleic acid synthesis.
Satellite DNA. A DNA fraction whose base composition differs from that of the main component
of DNA, as revealed by the fact that it bands at a different density in a CsCI gradient. Usually
repetitive DNA or organelle DNA.
Second messenger. A diffusible small molecule, such as cAMP, that is formed at the inner
surface of the plasma membrane in response to a hormonal signal.
Biochemistry-I
139
Secondary structure. In a protein or a nucleic acid, any repetitive folded pattern that results from
the interaction of the corresponding polymeric chains. In proteins, the most common are b-strands
(sheets) and a-helices.
Semiconservative replication. Duplication of DNA in which the daughter duplex carries one old
strand and one new strand.
Semipermeable. The characteristic of allowing only some molecules, usually smaller or
uncharged ones, to pass through.
Sigma factor. A subunit of RNA polymerase that recognizes specific sites on DNA for initiation
of RNA synthesis.
Signal sequence. A (usually N-terminal) sequence of a protein that directs its processing or
localization within the cell.
Single-copy DNA. A region of the genome whose sequence is present only once per haploid
complement.
Steroids. Compounds that are derivatives of a tetracyclic structure composed of a cyclopentane
ring fused to a substituted phenanthrene nucleus.
Structural domain. An element of protein tertiary structure that forms an independent folding
unit.
Structural gene. A gene encoding the amino acid sequence of a polypeptide chain.
Structural protein. A protein that serves a structural function.
Substrate. A molecule that is acted upon, and chemically changed, by an enzyme.
Subunit. Individual polypeptide chains in a protein.
Supercoiled DNA. Supertwisted, covalently-closed duplex DNA.
Template. A polynucleotide chain that serves as a surface for the absorption of monomers of a
growing polymer and thereby dictates the sequence of the monomers in the growing chain.
Termination factors. Proteins that are exclusively involved in the termination reactions of
protein synthesis on the ribosome.
Terpenes. A diverse group of lipids made from isoprene precursors.
Tertiary structure. In a protein or nucleic acid, the final folded form of the polymer chain.
140
Tetramer. Structure resulting from the association of four subunits.

Thymidine. One of the four nucleosides found in DNA.
Thymine. A pyrimidine base found in DNA.
Topoisomerase. An enzyme that changes the extent of supercoiling of a DNA duplex.
Transcription. RNA synthesis that occurs on a DNA template.
Transduction. Genetic exchange in bacteria that is mediated via phage.
Transfection. An artificial process of infecting cells with naked viral DNA.
Transfer RNA (tRNA). Any of a family of low-molecular weight RNAs that transfer amino
acids from the cytoplasm to the template for protein synthesis on the ribosome.
Transferase. An enzyme that catalyzes the transfer of a molecular group from one molecule to
another.
Transformation. Genetic exchange in bacteria that is mediated via purified DNA. In somatic cell
genetics the term is also used to indicate the conversion of a normal cell to one that grows like a
cancer cell.
Transgenic. Describing an organism that contains transfected DNA in the germ line.
Transition state. The activated state in which a molecule is best suited to undergoing a chemical
reaction.
Translation. The process of reading a messenger RNA sequence for the specified amino acid
sequence it contains.
Transport protein. A protein whose primary function is to transport a substance from one part of
the cell to another, from one cell to another, or from one tissue to another.
Tricarboxylic acid (TCA) cycle. The cyclical process whereby acetate is completely oxidized to
CO2 and water, and electrons are transferred to NAD+ and flavine. The TCA cycle is localized to
the mitochondria in eukaryotic cells and to the plasma membrane in prokaryotic cells. Also called
the Krebs or citric acid cycle.
Trypsin. A proteolytic enzyme that cleaves (cuts) peptide chains next to the basic amino acids
arginine and Iysine
Ultracentrifuge. A high-speed centrifuge that can attain speeds up to 60,000 rpm and centrifugal
fields of 500,000 times gravity. Useful for characterizing and/or separating macromolecules.
Biochemistry-I
141
Unwinding proteins. Proteins that help to unwind double-stranded DNA during DNA
replication.
UV irradiation. Electromagnetic radiation with a wavelength shorter than that of visible light
(200-390 nm). Causes damage to DNA (mainly by forming pyrimidine dimers).
van der Waals forces. Refers to the combined effect of two types of interactions, one attractive
and one repulsive. The attractive forces are due to favorable interactions among the induced
instantaneous dipole moments that arise from fluctuations in the electron charge densities of
neighboring nonbonded atoms. Repulsive forces arise when noncovalently bonded atoms come
too close together.
Vitamin. A trace organic substance required in the diet of some species. Many vitamins are
precursors of coenzymes.
Watson-Crick base pairs. The type of hydrogen-bonded base pairs found in DNA, or
comparable base pairs found in RNA. The base pairs are A-T, G-C, and A-U.
Western blot. Similar in principle to a Southern blot, but where the species adsorbed to the
nitrocellulose filter is a protein, and the detection makes use of specific antibodies.
Wild-type gene. The form of a gene (allele) normally found in nature.
Wobble. A proposed explanation for base pairing that is not of the Watson-Crick type and that
often occurs between the 3' base in the codon and the 5' base in the anticodon.
X-ray crystallography. A technique for determining the structure of molecules from the X-ray
diffraction patterns that are produced by crystalline arrays of the molecules.
Z form. A duplex DNA structure in which there is the usual type of hydrogen bonding between
the base pairs but in which the helix formed by the two polynucleotide chains is left-handed
rather than right-handed.
Zwitterion. A dipolar ion with spatially-separated positive and negative charges. For example,
most amino acids are zwitterions, having a positive charge on the a-amino group and a negative
charge on the a-carboxyl group but no net charge on the overall molecule.
Zygote. A cell that results from the union of haploid male and female sex cells. Zygotes are
diploid.
Zymogen. An inactive precursor of an enzyme. For example, trypsin exists in the inactive form
trypsinogen before it is converted to its active form, trypsin.
142
Top Ten Books for Biochemistry

1.
2.
3.
4.
5.
Principles of Biochemistry by Lehninger, Nelson & Cox.

Biochemistry by Lubert Stryer, Berg and Tymoczko.
Fundamentals of Biochemistry by Voet, Voet & Pratt.
Biochemistry by Garrett & Grisham.
Harpers Illustrated Biochemistry by Robert K Murray , Daryl K Granner ,
Victor W Rodwell.
6. Lippincott's Illustrated Reviews Biochemistry, 5/e by Harvey.
7. Principles and Techniques of Biochemistry and Molecular Biology by Keith
Wilson & John Walker (Eds.).
8. Fundamentals of Biochemistry by J.L.Jain.
9. Biochemistry by Geoffrey L. Zubay.
10.Text Book of Biochemistry by Dr. G. R. Agarwal, Dr. O. P.
Biochemistry-I
143
Notes
144
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2

Biyani's Think Tank

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Concept & Copyright :

Biyani Shikshan Samiti

Leaser Type Setted by :

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2. Enzymes: Nomenclature and classification, co-enzymes and co-factors, reaction and

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Concept of Life & Living Processes

Which statement is FALSE about nearly all living things?

What are the identifying characteristics of Living matter?

Living organisms are highly complicated and organized structures and

Each component unit of a living object appears to have specific purpose or

Write axioms or principles of Living State.

There is basic simplicity in structure of biological molecules.

Identities of each species or organism are preserved by its possession of

All biomolecules have specific functions in cells.

Living organisms create and maintain their complex, orderly, purposeful

Living cells are self-regulating chemical engines.

(viii) Genetic information is encoded in units that are submolecular in

It carries out various reactions catalyzed by biocatalyst or enzymes.

The energy needed is provided directly or indirectly by solar energy.

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Cell Membrane System & Cell Wall

D. vacuole, cell membrane, nucleus, mitochondria

b- are organized into polysomes in cells synthesizing intracellular proteins

Give brief account on Membrane Phospholipids?

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In addition to phospholipids plasma membrane of animal cells contains

Write short note on Membrane Proteins?

Peripheral proteins: Also called as extrinsic proteins; they do not interact

Integral membrane proteins: Proteins that held in bilayer by unusually

Following are the various Types of Integral Membrane Proteins:

Transmembrane Proteins: Most integral proteins span entire

Lipid Anchored Protein: Some proteins are anchored to membrane by

Write in detail about Mitochondria?

Ans.: Mitochondria were first observed by Kolliker as globular structure in striated

Inner Compartment or Matrix Space

Direct Observation of Mitochondria: Direct examination with vital stain

Cell Fractionation: Mitochondria can easily be isolated by differential

Cytochemical marking: Different parts of Mitochondria have distinct

Enzymes present in Mitochondria:

Enzymes on outer Membrane: Monoamine oxidase, cytochrome reductase,

Enzymes on Inner Membrane: ATP synthetase that makes ATP in inner

Enzymes on Inter membrane space: Enzymes require to phosphorylate the

Enzymes on Mitochondrial Matrix: Enzymes that required for oxidation of

Matrix contain: Malate dehydrogenase, Isocitrate dehydorgenase,

Describe structure and function of Golgi apparatus?

Tubules: Complex array of associated vesicles and anastomosing tubules.

Clathrin Coated vesicles: Spherical protuberance found at periphery of the

The GERL region: Golgi apparatus is spatially and temporally related to

Zymogen of exocrine pancreatics cells

Mucus secretion & goblet cells of intestine.

Also involved in formation of certain cellular organelles such as plasma

Describe structure and function of Endoplasmic Reticulum?

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