CYTOLOGY

THE CONCEPT OF CYTOLOGY.

Cytology is the study of cells, their structures, functions, characteristics and

adaptations. THE CELL THEORY

The bodies of all living things are made up of cells.

Robert Hooke (1665) was the first person to discover a cell from a plant cork. The cells looked
like boxes. Other people who studied the structure of cells are Lamark (1809), Detrochet (1824)
and Turpin (1826).

Schleiden (1838) studied the plant cells and emphasized that the cells are organisms and entire
animals and plants are aggregations of these organisms arranged according to the definite
laws.

In 1839 Schwann, a German botanist stated that ” we have seen that all organisms are composed
of essentially like parts namely of cells”.

IMPORTANCE OF CYTOLOGY

Cytology has been very important discipline in the research diagnosis and treatment of human
diseases. Most of health problems people encounter involve the cell disturbances.

The study examines cell interaction. Studying how cells interact or relate to other cells or
environments the cytologists can predict problems or examine the dangers to the cell and identity
type of infections.

THE MAIN IDEAS OF THE CELL THEORY

1. All organisms are made up of cells.

2. The new cells are derived from the pre-existing cells by the process of cell division (mitotic
and meiotic division).

3. All chemical reactions/metabolic activities in the bodies of the organisms take place within the
cells.

4. The cells contain hereditary materials which are passed from one generation to

another. 5. Given a suitable condition, a cell is capable of independent existence.

CHALLENGES OF THE CELL THEORY

 • Hereditary materials are also found in viruses, mitochondria and chloroplasts, all of
which are not viruses.

STRUCTURE OF CELLS AND FUNCTIONS

The five structures are also known as ultra structure and are obtained by two techniques.

• Physiological or metabolic activities take place within a cell. Viruses though are not cells,
have life within their hosts.
• The new cells arise from pre-existing cells by cell division. In this postulate the theory
does not specify about the origin of the first cell.
• All living things must have cells. This postulate is challenged by the existence of viruses,
where when they are inside the body of their host, viruses act as living things even
though they don’t have cellular organization.
• Electronic microscope.
• Cell fractionation.

A cell is usually a tiny, three dimensional sac of many organelles which are suspended
within an aqueous medium (the cytoplasm) containing or contained (bounded) by a cell
membrane.

In the case of plants, a cell wall is bounded by a cellulose cell wall.

The bulk of these structures (organelles) of the cells is referred to as a

cytoplasm. Cytocil is the fluid part of the cytoplasm.

PROKARYOTIC CELLS.

They are extremely small for example bacteria all range from 0.5 – 10

micrometers. They appeared about 350 million years ago.

Cells of prokaryotes lack the true nuclei that are their genetic material (DNA) are not enclosed
by the nuclear membrane and lies freely in the cytoplasm.

EUKARYOTIC CELLS

The cells of eukaryotic have three basic parts

1. The plasma membrane.

2. The cytoplasm.

3. The nucleus.
Plasma membrane.

This is also called the cell surface membrane as plasma membrane or plasma lemma which
separates the contents of the cells from the external environment, controlling the exchange of
materials.

In animal cells it is an outermost layer where as in plant cells it is beneath the cell wall. E.g.
neurillema in neurons.

Muscle cells – sacrolemma.

STRUCTURE OF THE CELL MEMBRANE

There are two models suggested by different scientist to try to describe the cell

membranes. These are;

i. Daniel-Davson model (1935)

ii. Fluid mosaic model (1972)

Daniel-Davson model

Diagram

According to Daniel and Davson, the membrane is structurally composed of two chemical
substances that form their own layer.

1. Protein layer made up of molecules. The layer is continuous and lacks pores.

2. Phospholipids (at least two layers of phospholipids) oriented with their polar (hydrophilic ends
near the surface and their non polar (hydrophobic) hydrocarbon chains in the interior of the
membrane as far as possible from the
surrounding water.

According to the model, the membrane is structurally rigid static and non

dynamic. Strength of the model.

1. The model suggests that the membrane is composed of proteins and lipids.

2. Ampliphetic (double) nature of phospholipids such as phospholipids molecule has a polar head
(hydrophilic) and a non polar tail (hydrophobic).

WEAKNESS OF THE MODEL

1. The model suggests that the protein layer is continuous. Researches done by scientists show
that the protein layer is in-continuous.

2. The membrane is static is a wrong concept since the membrane is a dynamic ever changing
structure.

3. Lack of pores in protein layers.

The protein molecules in a membrane have pores for passage of materials.

4. The model does not indicate the presence of a carbohydrate.

THE FLUID MOSAIC MODEL.

The model was put forward by singer and Nicolson 1972 in order to modify the Daniel and
Davson model.

According to the fluid mosaic model, the membrane is an ever-changing structure in which the
mosaic protein floats on the lipid bilayer acting as a fluid.

Proteins in this model do not form a continuous layer covering both sides of the membrane as
proposed by Daniel and Davson model.

According to this model, the membrane has 3 constituents.

• Lipids (45%)
• Proteins (45%)
• Carbohydrates (10%)
1. Lipids.

There are two types of lipids.

a. Glycolipids;

These are lipids associated with short carbohydrates chain.

ROLES OF GLYCOLIPIDS

Cell to cell recognition.

Act as receptors for chemical stimuli.

b. Phospholipids;

These are lipids associated with phosphates. They form 2 layers i.e. phospholipids bilayer. Each
phospholipid consists of a polar head (hydrophilic) and a non polar tail (hydrophobic). Act as a
fluid and move about rapidly in their own layer. Since phospholipids are constantly in motion,
the membrane is described as being fluidly.

ROLES OF PHOSPHOLIPIDS

1. Form the basic structure of the membrane.

2. Determine the fluidity of the membrane.

3. Allow the passage of fat soluble substances.

NB: cholesterol is a type of steroid located in between phospholipids keeping them

fluidly. ROLES OF CHOLESTEROL

1. Disturb the close package of phospholipids keeping them fluids.

2. Increase the flexibility of the membranes by allowing relative movements of the bilayers
without actual displacement because it acts as an unsaturated fatty acid lubricating bilayer.

2. PROTEINS

These exist as globular in the membrane, i.e. they never form a continuous layer.

Within protein molecules or between adjacent there are poles. These may either be hydrophobic
or hydrophilic.
Since the phospholipids are always in constant motion (fluid) proteins float in it forming a fluid
mosaic model. The proteins are organized in a particular pattern known as mosaic.

There are protein molecules that extend/ transverse both layers of membranes. Other proteins are
partially embedded in the membrane. These are called intrinsic proteins.

Some proteins float freely inside the membrane, hence they are called peripheral or extrinsic
proteins.

TYPES AND ROLES OF PROTEINS.

1. Carrier proteins or channel proteins.

These are involved in the selective transportation of polar molecules. i.e. ions across the
membrane

e.g. movement of glucose to the cell, chlorine ions. (Cl-)

2. Enzymes

Catalyze different metabolic reactions.

3. Receptor molecule.

Some act as receptors for chemical stimuli example hormones.

4. Antigen.

Identity markers. These are glycoprotein. They have different shapes in every kind of a cell.
They have specific side chains thus are recognized by other cells and behave in an organized
manner.

5. Energy transfer.

In some physiological processes such as photosynthesis and respiration, some proteins are
involved in energy transfer (special form of membrane found in chloroplasts and
mitochondria).

3. CARBOHYDRATES

These branches to the outside of the membrane as an antennae or feelers.

There are two types;

1. Glycoprotein ( carbohydrate chain – plus protein)

2. Glycolipids ( carbohydrate chain plus lipid)
 They form a layer of glycocalyx

ROLES

1. Cell to cell recognition (in making tissues since same cells combine so similar cells will
have similar glycolipids/ glycoprotein).
2. To receive chemical stimuli.

STRENGTH OF FLUID MOSAIC MODEL.

1. It realizes the presence of phospholipids bilayer and protein layer.

2. The presence of polar head (hydrophilic) and non polar tail (hydrophobic) in the
phospholipids.
3. It shows that the membrane is not static.
4. It shows the presence of carbohydrates.
5. It shows that the protein layer is not continuous.
6. It indicates the presence of pores in the membrane passage of materials.

Diagram

FUNCTIONS OF CELL MEMBRANES.

1. It protects the cytoplasm contents of the cells.

2. It allows passage of materials in and out of the cells since it has pores.
3. In some membranes e.g. those of the intestine cells, there are microvilli which increase
the surface area for absorption of materials.
4. Acts as receptor sites for chemical stimuli such as hormones.
 5. In nerve cells, the membrane is over lined with a fatty sheath (myelin sheath) which
prevents the spreading of local currents to other neurons.
6. It aids cell to cell recognition when membranes of two cells come together.

VARIOUS WAYS BY WHICH MATERIALS PASS THROUGH THE

MEMBRANES. 1. Permeability

The plasma membrane is a thin elastic membrane around the cell which usually allows
the movement of small ions and molecules of various substances through it. This nature
of plasma membrane is termed as permeability.

2. Osmosis

The plasma membrane is permeable to water molecules. To and fro movement of water
molecules through the plasma membrane occurs due to the difference in concentration of
the solutes on its either side. The process by which the water molecules pass through a
membrane from region of higher water concentration to a region of lower water
concentration is termed as osmosis.

3. Diffusion or passive transport.

The diffusion of a certain solute or substance takes place through the plasma membrane
depends on the concentration and electrochemical gradient.

4. Active transport.

When molecules or ions move through the plasma membrane from low concentration to
higher concentration, they require energy for such movement.

The energy is provided by ATP which is produced by the mitochondria.

Through the pores of plasma membrane some chemicals such as urea and glycerol could
pass. It has been shown that large molecules of certain proteins also penetrate the cell.

5. Endocytosis and exocytosis.

The plasma membrane particles actively in the ingestion of certain large sized foreign or
food substances.

The process by which the foreign substances are taken and digested is known as
endocytosis.
 In the process of exocytosis, the cells which have secretory functions such as pancreatic
cells pass out their enzyme secretions outside the cell.

According to the nature of the food of foreign substance, endocytosis may be classified
into two types;

1. Pinocytosis

When the ingestion of food materials in bulk takes place by the cell through the process
known as pinocytosis.

2. Phagocytosis

Sometimes the large sized solid food or foreign particles are taken in by the cell through the
plasma membrane. The process of ingestion of large sized solid substances by the cell is
known as phagocytosis.

Question: what is the significance of a fluid mosaic model in the plasma membrane?

Ans:

• It explains easily the known physical and chemical properties of the membrane.
• It is the starting point to understanding the fix of the cell.
o All membranes of the cell plus the tonoplast and those of the organelles have the
fluid mosaic construction.

NB: this point provides the clues about the distribution of cell membrane in the
cell and its organelles.

NOTE:

Where

R=
rate of transport of material.

A = cross section surface area.

 CYTOPLASM

This is the part of a cell, which is filled with fluid in the protoplasm. This part of
the cell is the ground substance of the cell known as the hyaloplasm, where the
cell organelles are suspended. Cytosil is the soluble part of the cytoplasm.

Cytoplasm is distinguished into the following structures

1. Cytoplasm matrix

The space between plasma membrane and nucleus is followed by a morphous,

translucent, homogenous liquid known as cytoplasm matrix and hyaloplasm.

The cytoplasm matrix consists of various inorganic compounds e.g.

carbohydrates, lipids, proteins, nucleon proteins, nucleic acids (RNA and DNA)
and variety of enzymes.

The peripheral layer of a cytoplasm matrix is relatively non-glandular viscous and

known as endoplasm.

2. Cytoplasm inclusion

The cytoplasm matrix contains many refractive granules of various sizes; these
granules in the animal cells are known as cytoplasm inclusion.

The cytoplasm inclusion includes oil drops, yolk granules, pigments, secretory
granules and glycogen granules.

Such granules in plant cells are known as plastids. The most common plastids are
the chloroplasts (containing pigment chlorophyll), the leucoplastids (white color
plastids) ,omyplastids ( the plastids that store starch) and lipoplastids ( which
contain fats).

NB: plastids like cytoplasmic inclusion having only storage functions but also
perform various important synthesis and metabolic activities such as the
production of food materials due to the presence of chloroplasts.

ANIMAL CELL STRUCTURES

Diagram of the animal cells under light and electron microscope.

DIAGRAM OF ANIMAL CELL UNDER ELECTRON MICROSCOPE

ANIMAL CELL STRUCTURES

Characteristics;
 1. Have irregular shape.
2. Have centrioles.
3. Have lysosomes.
4. Lack cell walls.
5. Lack plastids.
6. Store carbohydrates in the form of glycogen e.g. phagocytotic vacuoles,
pinocytotic vacuoles, autophagic vacuoles and etc.
7. Cytokinesis occurs by furrowing i.e. periphery – centres direction of
constriction of cell membrane.

STRUCTURE OF THE PLANT CELL

A plant cell is incased in a tough and rigid cellulose cell wall.

Beneath the cell wall is the cell surface membrane which surrounds the cytoplasm.

The latter contains organelles; the prominent being vacuole plastids e.g. chloroplasts and
nucleus.

-Since a greater part of the cell is occupied by the vacuole, then the cytoplasm and nucleus are
squeezed by the vacuole to the periphery.

-When viewed under light microscope; only a few structures are seen under high magnification
power, even finer details are seen.

Diagram
Diagram of a plant cell under light microscope
CHARACTERISTICS OF PLANT CELLS

1. It has a fixed shape.

2. It has a cell wall made up of cellulose.
3. It has large permanent vacuole,
4. It has plastids; chloroplasts, chromoplast and leucoplasts.
5. Stores carbohydrates in the form of starch.
6. Lack lysosomes.
7. Lack centrioles.
8. Cell division; cytokinesis follows cento-periphery direction.

Similarities between a plant and an animal cell:

Both Have;

1. Plasma membrane
2. Distinct nucleus
3. Ribosome
4. Endoplasmic reticulum
5. Cytoplasm
6. Golgi apparatus
7. Qn What is an organelle?

An organelle is a distinct part of a cell which has a particular structure

and function e.g. Mitochondria, chloroplast, ER etc.
 CELL WALL

Cell wall is the structure that occurs externally to the cell.

Organisms with cell wall include.

8. Bacteria - have cell wall made up of murein and peptidoglycogen.

9. Fungi – has cell wall made up of chitin.
10. Algae and plant have cell wall made up of cellulose.

Plant cells cell walls.

It is the structure external to the cell; it isn’t an organelle although it is a product of various cell
organelle e.g. microtubules and Golgi apparatus.

CHEMICAL COMPOSITION.

It is made up of cellulose (mainly fibres) forming amorphous matrix of the cellulose that
surrounds the entire cell.

Such fibre is made up of several hundred microfibrils which form the network of cell wall.

In addition to cellulose plant cell wall consists of pectron and hemicellulose which contribute to
mechanical strength of the organism.

Pectron

These are polysaccharides of galactose and galactronic acid. Pectron may combine with Ca 2+
or Mg2+ to form calcium pectate or magnesium pectrate, which are important components of
the first layer of cell wall to be laid down on middle lamella.

Hemicellulose

Hemicellulose is the mixture of many compounds, but the chief ones are sugar e.g. glucose and
sugar acid residue.

Hemicelluloses which form hydrogen bounds with cellulose fibres in the cell matrix. The cell
wall is usually modified by deposition of other substances such as alginic acid and calcium
carbonate in the case of algae.

Functions of cell wall.

1. Mechanical support and skeletal support of individual cell and plants as

well. This is through lignifications.
2. To prevent cell from bursting in hypotonic solution.
3. Control cell growth and shape. Orientation of cellulose microfibrils limits
and helps to control cell growth and shape because of the cells ability to
stretch is determined by their arrangements.
4. Movement of water and material salts.

The system of interconnected cell walls (apoplast) is a major pathway of

the movement of water and dissolved mineral salts.

The cell walls are held together by middle lamellae, they also posses
minute pores through which structures called plasmodesmata form living
connections between cells and allows the protoplast to be linked in a
system called symplast.

5. Reduction of water loss and reduced risk of infection (due to its waxy
cuticle).
6. Transportation of materials. The walls of xylem vessels and sieve tubes
are adopted for long transportation of materials through the cells.
7. Barrier to water movement.

The cell walls of root endodermal cells are impregnated with suberin that
forms a barrier to water movement.

8. Some cell walls are modified as food reserves as in the storage

hemicelluloses in some seeds.
9. Transport of materials by active transport.

The cell wall of transfer cells develops an increased surface area and this
increases the efficiency and transfer materials by active transport.

CELL ORGANELLES OR ORGANOIDS.

Besides the cellular inclusion and plastids, the cytoplasm matrix contains many large sized
structures known as cell organelles or organoids which perform various important synthesis,
transportation, support and

reproduction.
These organelles are the endoplasmic reticulum, ribosome, Golgi complex, liposomes,
mitochondria, plastids, centrioles, cilia etc.

Functions of cytoplasm

1. It provides medium for chemical reaction to take place like protein synthesis, lipids
synthesis and etc.
2. It stores useful materials such as amino acids, proteins, starch, carbohydrates, lipids, O2
etc.
3. It stores waste materials such as C02 and nitrogen waste etc.
4. It controls the absorption of materials across the membrane due to its concentration
gradient.

CELL ORGANELLES

1. ENDOPLASMIC RETICULUM

Is the cytoplasm matrix, is transverse by a vast reticulum or network at interconnecting

tubules and vesicles which is known as endoplasmic reticulum or ER.

The endoplasmic is having a single vast and interconnected cavity which remains
bounded by a single membrane. The membrane of endoplasmic reticulum is supposed to
be originated in pushings of plasma membrane

in the hyloplasm (matrix) because chemically it consists of a lipoproteinous structure like

plasma membrane.

The membrane of the endoplasmic reticulum may be either smooth when they do not
have attached ribosome and rough when they have the attached ribosome.

The membranes of endoplasmic reticulum are found to be continuous with the nuclear
membrane and plasma membrane.

FUNCTIONS OF ENDOPLASMIC RETICULUM

1. Transport of materials from exterior to the nucleus or to cytoplasm organelles such as

Golgi complex.
2. It provides mechanical support to the cytoplasm matrix.
3. Functions as a cytoplasm framework.

Surfaces for some of the biological activities of the cell catalyst its complex folding
provide an enormous surface for such activities.
4. Synthesis and transfer of lipids.( smooth endoplasmic reticulum)
5. In the liver the smooth endoplasmic reticulum detoxifies many poisons and drugs. 6. The
rough endoplasmic reticulum transports proteins synthesized in the ribosome of the rough
endoplasmic reticulum.
7. Formation of Golgi bodies as they are modified endoplasmic reticulum.
8. Routes for movement of materials from the nucleus to the cytoplasm.

2. GOLGI APPARATUS/ DICTYLOSOMES This cell organelle is also known as the

Golgi body, Golgi complex or sityasome.
It is the apparatus which consists of membranous sacs called cisternae and a system of small
vesicle (called Golgi vesicles or dictysome vesicles) and vacuoles of various sizes.

The membranes of Golgi complex are of lipoproteins and these are supposed to be originated
from the membrane of endoplasmic reticulum.

FUNCTIONS

1. Produce secretions

There are many Golgi apparatus in;

• Cells of salivary gland

• Cells of root cap
• Cells of endocrine glands i.e. pancreas

2. Modification of materials.

The combination of carbohydrates and proteins to form glycoprotein takes place in them.
Many materials such as mucin are glycoprotein. It takes place in the cistern.

Carbohydrate chain + lipids = glycolipids

3. Production of carbohydrates example cellulose produced in plants after division. Thus

this separates one cell from another.

4. Transport of lipids (storage and transport of proteins and lipids) after digestion, the
fatty acids and glycerol are formed. In the endoplasmic reticulum fatty acids and glycerol
unite to form lipids (triglycerides). The latter are passed to the Golgi apparatus where it
 transports them to the plasma membrane as lymphatic system and going to the lymphatic
system.

5. Formation of lysosomes.

6. Synthesis of various types of carbohydrates from simple sugars.

7. It activates the mitochondria to produce ATP.

8. It forms the acrosome of the sperms.

3. LYSOSOMES.

These are spherical single membrane bound organelles containing digestive

enzymes. -lipase

-carbohydrases

- Nucleases

The enzymes are synthesized in ribosome RER transported to the Golgi apparatus for
modification. The Golgi vesicles are detached from the Golgi apparatus and remain in the
cytoplasm as lysosomes because they contain digestive enzymes.

FUNCTIONS

1. Functions as storage vesicle for many powerful digestive (hydrocytic) enzymes.

2. Acts as digestive system of the cell enabling it to process some of the bulk materials taken in
by phagocytosis or pinocytosis. Digests parts of the cell such as worn out organelles and also to
digest the stored food contents of chloroplast A and B in extracellular digestion.

3. Play role in some developmental process e.g. remolding of bones and fractures.

NB: in plant cells, the large contrast vacuole may act as lysosomes although bodies similar to
lysosomes of an animal cell sometimes seen in the cytoplasm of a plant cell.

4. RIBOSOMES.

Structurally it has two sub-units, i.e. small subunit and large subunit.
Each of the two subunits is composed of rRNA (ribosomal RNA) and proteins.

It is present in both eukaryotic and prokaryotic cells. The sizes can be determined by the
sedimentation when centrifuging showing the 80’s and 70’s ribosome.

-80’s ribosome are present in R.E (rough endoplasmic) reticulum of eukaryotic cells.

-70’s ribosomes are present in prokaryotes as well as mitochondria and chloroplasts of

eukaryotic cells.

FUNCTIONS OF RIBOSOMES

1. They provide large surface area for protein synthesis.

2. They are binding sites of the RNA.

ADAPTATIONS OF RIBOSOMES.

The ribosomes are the sites for protein synthesis. it has the following characteristics.

1. Presence of enzymes capable of catalyzing the synthesis of peptide bonds.

2. Presence of ribosomal RNA (rRNA) that attract other types of RNA i.e. mRNA and
tRNA towards the ribosome’s.

5. VACUOLES

1. A vacuole is a fluid filled sac which is bound by a single membrane.

In animal cells, there are relatively small and temporary vacuoles such as phagocytotic,
pinocytotic, autophagic vacuoles in plant cells; the vacuole is large and occupies a greater
proportion of the cytoplasm.

The membrane bounding the vacuole is the tonoplast and the fluid inside is the cell sap or
vacuole sap.

The cell sap is a mixture of many substances; concentrates solutions of sugar, salt,
organic acids, gases such as C02 and oxygen, pigments and waste products of
metabolism.
 It also contains enzymes similar to those of lysosomes.

ROLES OF CELL VACUOLES

1. They are involved in primary plant growth. It is a result of turgor pressure generated inside the
vacuoles as a result of entry of water. This causes cell expansion as the tonoplast is pressed
against the cell wall.

2. The pigment contained in the cell sap is responsible for flower color and therefore play a key
role to pollination.

3. They contain enzymes similar to those of lysosomes when plant cell dies. The tonoplast looses
the differential permeability and enzymes escape causing autolysis.

4. Vacuole acts as a temporary store of waste products such as crystals of waste calcium oxalate,
toxins and metabolic waste products of plants.

5. The vacuoles sometimes functions as food reserves e.g. sucrose mineral salts and insulin are
stored in vacuoles.

6. In prokaryotes it serves for buoyancy.

6. MITOCHONDRIA

Structure of mitochondria

It is a sausage shaped or an oval shaped organelle surrounded by a double membrane

(mitochondrial envelope). The envelope consists of the outer and inner membrane.

Between the two membranes there is a space, the intermembranal space.

The outer membrane is smooth while the inner membrane is coiled to form t=surface area for
attachment of membranes.

The ground substance of the mitochondrion is called matrix. This contains

1. Several enzymes responsible for Krebs cycle.

2. Circular DNA that resembles that of prokaryotic cells. It is for self replication of
mitochondria.

3. 70s ribosome like those of prokaryotic cells. These are for protein synthesis e.g. enzymes
 Diagram of mitochondrion

Functions of mitochondrion

The main function of mitochondrion is to yield energy during respiration.

About 98% of energy is synthesized e.g. one molecules of glucose yield 38 ATP. Out of
38ATP 36 is synthesized in the mitochondrion by the reactions of Krebs cycle and
electron transport chain. Thus it is called power house or POWER station or power plant
of the cell.

Adaptations of the mitochondrion to energy productio

1. Presence of outer membrane and inner membrane to allow entry and exit of materials.
2. The inner membrane is coiled to increase the surface area for attachment of enzymes
responsible for electron transfer.
3. Presence of matrix which is as granular and gives enough space for reaction to take place
(Krebs cycle reaction) also matrix contains Krebs cycle enzymes.

4. Presence of circular DNA for replication of the mitochondrion.

5. Have 70s ribosome’s for synthesis of proteins.
6. Presence of phosphate for production of ATP.
7. Presence of Oxysome and water accompany aerobic respiration.

NB: the inner folded to form partitions called cristae which enables different types of metabolic
activities to take place. This phenomenon is called compartmentalization hence enables multi
enzymes systems to operate.

ENDOSYMBIOTIC THEORY

(Evolution of mitochondria)

The mitochondria were originally independent prokaryotic bacteria like organisms which entered
hosts cells and develop mutual relationship (symbiosis).

MITOCHONDRIA AS PROKARYOTIC CELL

1. Posses its own DNA and is able of self replication / reproduction.

2. Have a circular like bacteria DNA.
3. It is sensitive to different antibiotics such as chlorophyll and streptomycin which inhibit
mitochondrial activities.
4. It contains ribosomes similar to those of bacteria.

7. PLASTIDS

These are organelles with double membrane, located in plant cells and algae

Types

1. Chromoplasts
2. Leucoplasts
3. Chloroplasts

1. CHROMOPLASTS

(Chromo – color / pigment)

These are types of plastids bearing pigments i.e. yellow, red, orange, purple

pigments. Found in

1. Flowers
2. Fruits
3. Seeds
4. Leaves
5. Roots of carrots.

2. LEUCOPLAST (embryos and germ cells)

 Leuco- colour / white.

These are colour plastids found mainly in storage organs. There are various types of
leucoplasts;

1. Amyloplasts- contain starch

2. Lipoplasts – stores lipids
3. Proteoplasts- stores proteins

Structure of chloroplasts

The chloroplast

-the chloroplast is an oval shaped green in color due to presence of chlorophyll.

- It has two membranes an outer and an inner membrane which constitutes the double membrane
or chloroplast envelope.

-Between the membranes there is the inter membrane space.

- The ground substance of the chloroplast is the stroma.

- The latter has a system of parallel running membranes called thylakoids.

-the interval between one grannum and the other is called intergranal lamellae. - The

stroma contains circular DNA and fewer small 70’s ribosomes and starch granules.

Functions of chloroplasts

1. It is the site of photosynthesis.

This is the process whereby green plants manufacture food from CO2 and water in the
presence of light energy, it stores starch temporarily.

2. The thylakoids have chlorophyll pigment for trapping sunlight energy.

3. It has grana and thylakoids to hold the chlorophyll in proper position for maximum
absorption of light energy.
4. Stroma contains enzymes for dark reactions of photosynthesis.
5. Presence of phosphate which acts as a source of phosphate during phosphorylation.
6. Ribosomes and circular DNA for synthesis of proteins such as enzymes

Endosymbiotic nature of chloroplasts and mitochondria.

 The chloroplast and the mitochondria are endosymbiotic structures within a cell. They are
capable of leading life within a cell because;

1. They have double membrane which allows passage of materials in and out of their inside.
2. They have their own hereditary materials i.e. circular DNA. They are capable of self
replicating.
3. They have ribosomes (70’s) thus synthesize proteins. E.g. enzymes.
4. Have matrix or stroma, the ground substance where various reactions take place.

STROMA; various photosynthetic membrane are found where light reactions take place
and dark reactions in the aqueous part.

MATRIX: Krebs cycle of respiration.

5. They have their own enzyme system.

Therefore chloroplasts and mitochondria are said to be cells within cells.

The endosymbiotic nature of chloroplasts and mitochondria can be described as serial

endosymbiotic theory (SET).

SERIAL ENDOSYMBIOTIC THEORY.

This theory accounts for the evolution of eukaryotic cells from prokaryotic

cells. Evidence / similarities of organelle and prokaryotic cells

• Double membrane as cell membrane.

• Circular DNA.
• 70’s ribosomes.
• System of enzymes.

SERIAL ENDOSYMBIOTIC THEORY.

It was suggested that mitochondrion, chloroplasts are descendants of ancient prokaryotic

organisms.

-Eukaryotic cells arose from invasion of one large cell by other prokaryotic

cells. The SET states that;

“All eukaryotic cells contain genetic material (DNA) ribosomes that resemble those of
prokaryotic cells’’.

-It suggests that prokaryotic heterotropes ingested other mitochondrion like prokaryotic and
roughly at the same time began forming an organized nucleus.

Subsequently, non motile cells established a symbiotic relationship with yet another prokaryote
in the form of spirochetes or spiroplasma bacterium, attached to the outside of the cell. Such as
bacterium has a function like flagellum.

Eventually a photosynthetic prokaryote engulfed by this regardless as a primitive plant cell.

QNS

1. Chloroplasts, mitochondria and bacteria have features in common. Enumerate the

features to reveal the truth of this statement.
2. Where in the body would you expect to find large number of mitochondria? Give
reasons.
3. If mitochondria were to perform the function of the function of the chloroplast, what
modification would it require.

8. MICROBODIES OR PEROXISOMES

These are small spherical bodies with 0.5 – 1.5 micrometers in diameter. The ground substance
of a micro body contains important enzymes especially catalyze or peroxidase.

These enzymes catalyse the hydrolysis of hydrogen peroxide in water and

oxygen. These peroxisomes are found in liver, potatoes, pea seeds and bean seeds.

Diagram
FUNCTIONS OF PEROXISOMES

1. To break down the poisonous hydrogen peroxide to water and oxygen in the presence of
peroxidase enzyme/ catalase.

2. In plants special peroxisomes called glycoxisomes are centre’s for glycoxylate cycle i.e.
conversion of fats into carbohydrates especially during germination.

3.The leaf of peroxisomes are centers of photorespiration, especially in C3 plants e.g. beach
plants, potato plant, tomato, coffee in cold areas.

CYTOSKELETON

This is a complex network of fibrous protein structure that exists in cytoplasm of eukaryotic cell
and anchor proteins or organelles such as nucleus to their fixed location.

The structures which constitute cytoskeleton include;

1. Microfilament( actin filaments)

2. Intermediate filaments
3. Microtubules

1. MICROFILAMENTS(ACTIN FILAMENTS)

These are thread like structures arranged in sheets or bundles first beneath the cell surface
membrane.

Diagram
-Chemically they contain actin and myosin.

-Each fibre is composed of two chains of protein loosely twisted about one another in helical
manner. These proteins molecules can be assembled and dis-assembled.

FUNCTIONS

• Interactions of these fibres with myosin help in muscle contraction.

• Determine the shape of cell’s skeleton.
• Responsible for movement of materials within the cells.
• Cleavage of animal cells is brought about by the constriction of a ring of microfilaments
after nuclear division, cytokinesis.

2. INTERMEDIATE FILAMENTS.

These are structures intermediate between microtubule and microfilament (rope like
microtubule of polypeptides)

Skin cells for example form intermediate filaments from proteins called KERATIN. When the
skin dies the intermediate filament of the cytoskeleton persists.

Hair and nails are formed this way.

FUNCTION

1. Provide cells shape

2. Act as intercellular tendons preventing excessive stretching of cells.
 3. MICROTUBULES

Microtubules are tubular structures made up of helizelly arranged globular subunit called tubulin.

-They are about 25 nm in diameter. Each has a chain of proteins wrapped round and round in a
tight spiral. Large microtubules are found in cilia, flagella, centrioles (formation of spindle
fibres microtubules).

Functions

1. They bring about movement of chromosomes during metaphase in nuclear division. 2.

Since they are tubular, they transport materials from one part of the cytoplasm to another, i.e.
they are cytoconductors.
3. In cilia and flagella, they help in rhythmical beating up movement.
4. They determine the shape of the cell. (Skeletal support).

9. CILLIA AND FLAGELLA.

The cells of many unicellular organisms and ciliated epithelium of multi-cellular organisms
consists of some hair like cytoplasm projections outside the surface of the cell.

-These are known as cilia or flagella and they help in locomotion of the cells. The cilia and
flagella are made up of proteins adenosine triphosphate (ATP).

-In prokaryotic cells, cilia and flagella (If they have structure lacking 9+2 arrangement of
microtubules and arise from basal bodies).

-In eukaryotic cilia and flagella are complex. They have the 9+2 arrangement of microtubule and
arise from basal bodies.

10. CENTRIOLES.

Centrioles are present in animal cells only.

-They are two placed at right angle to each other.

-A number of rays called ultra rays usually surround the centrosomes.

Each centriole is composed of nine paired thin threads and is in the form of

cylinder. They aid in cell division.

11. PINOCYTOTIC VESSICLE

These are organelle formed as a result of in folding of plasma membranes as it takes large
particles of food from outside the cell.

The process is called pinocytosis.

Eventually pinch off and form very small vacuole (vesicle).

FUNCTIONS

Transport large particles into the cell.

12. NUCLEUS.

-Nucleus is the functional unit of a cell.

It contains materials which control different activities within the cell; the genetic materials.

STRUCTURE OF THE NUCLEUS.

The nucleus has a membrane called nuclear membrane envelope.

Then nuclear membrane has some pores which allow some materials to pass in and out of
nucleoplasm to allow communication on with cytoplasm called nuclear pores.

-Nuclear pores are made up of non-membrane materials forming nuclear pores.

-Nuclear envelope is semi permeable membrane allowing some materials to pass and others not
to pass.

-The space inside the nucleus is filled by fluid materials which are called nucleoplasm. These are
semisolid granules ground substance or matrix.

Within the nucleoplasm there are two components;

1. Nucleolus
2. Chromatin
3. Matrix (aqueous)

Chromatin threads
 Chromatin threads are grainy network of strands that undergo cooling into rod-like
structures called chromatin.

Chemically chromatin and therefore chromosomes contains DNA (deoxyribose nucleic

acids) and much protein and some RNA (ribonucleic acids) and few minerals.

Nucleolus

These are small dark regions where different RNA type examples ribosomal RNA is
produced and RNA joins the protein to form the subunit of ribosomes.

-It synthesizes the ribosomes protein and is used in controlling the cell division.

Functions of nucleolus

1. Controls all metabolic activities of the cells

2. It regulates cell division.
3. Concerned with transmission of hereditary traits from parent to offspring.
4. Synthesizes and stores proteins.

PROKARYOTIC CELL

1. A WELL LABELLED DIAGRAM OF A BACTERIAL CELL.

 PROKARYOTIC CELL e.g. EUKARYOTIC CELL e.g.
bacteria, cyano bacteria. protoctista, green plants, animal and
1. Usually extremely small cells. fungi.

Usually large cells about 10-100 micrometer

2. Nucleus absent, naked circular DNA Distinct nuclear region DNA helical
shaped enclosed in a protein coat.
3. No nucleus.
Nucleus present
4. Few organelles and non are surrounded
by an envelope (double membrane). Many organelles envelope(bound)
5. Internal membrane if present usually organelles ( i.e. double membrane bound
associated with respiration or organelles)
photosynthesis. Great diversity of internal membrane
6.Flagella are simple lacking arrangement organelle e.g. Golgi apparatus, lysosomes,
of microtubule. ER.
Complex flagella with ( 9+2) arrangement
7. Have mesosome for respiration.
of microtubule.
8. Some are nitrogen fixing.
Use mitochondria for respiration
9. 70’s ribosomes.
No ability to fix nitrogen.
80’s ribosomes

Similarities between prokaryotic and eukaryotic cells.

Both have;
 1. Structure for movement (cilia and flagella)
2. Cell wall.
3. Cell membrane.
4. Ribosome’s.
5. Genetic material.(DNA)
6. Storage of food organelles.

QUESTIONS

1. a. Give the principle constituent of the cell membrane.

b. Draw a fully labeled diagram to illustrate the arrangement of these constituents and
others in the fluid mosaic model of the cell wall membrane.

c. why is the model described as being fluidy?

d. Give two functions of the cell membrane.

2. Describe the role of the following membranous organelles; lysosomes, endoplasmatic

reticulum, ribosome’s and Golgi apparatus.

CELL DIFFERENTIATION

This is the specialization of a cell in terms of both structure and functions. Ability of a cell to
perform single function is called cell specialization. Cells work in interdependence with each
other such that such that group of cells must be coordinated so that they carry out their activities
efficiently such coordination is called integration.

CYTOLOGY 2
BIOCHEMISTRY

ORGANIC CONSTITUENT OF THE CELLS.

Bio chemistry: is the study of structures, properties and functions of chemical constituents of the
cells.

-It is a great unifying theme in biology.

It finds applications in fields like;

1. Agriculture; in developing pesticides and herbicides.

2. Medicine; including all pharmaceuticals.
3. Fermentation; baking products, food products and breweries.
4. New development of biology eg genetic engineering.

ELEMENTS FOUND IN LIVING ORGANISMS ARE

1. Chief/ macro elements: hydrogen (H), carbon(C), nitrogen (N), oxygen (O),
phosphorous (P), sulphur(S).
2. Ions – sodium(Na+) , magnesium (Mg2+) , chlorine( cl-) , calcium (Ca2+) etc. 3. Trace
elements – manganese(Mn) , iron(Fe) , cobalt(Co),copper (Cu) , molybdenum(Mo) and
iodine(I).

MACROMOLECULE(S)

Macromolecule is a giant molecule made from many repeating units. The molecules built are
polymers and the individual units are monomers.

-The units are joined together by a chemical process called CONDENSATION which means
removal of water.

-The units can be broken down again by an opposite process known as hydrolysis which means
adding of water.

• The most important macromolecules in biology are;

1. Polysaccharides( carbohydrates)
2. Protein
3. Lipids
4. Nucleic acids.

And their constituent monomers are; monosaccharide’s, amino acids, glycerol, fatty acids and
nucleotides respectively.

Others are;

• Adenosine triphosphate (ATP).

ORGANIC SUBSTANCES ( CHEMICAL NATURE AND

IMPORTANCE) 1. CARBOHYDRATES

They are substances which contain carbon, hydrogen and oxygen with the general formula of
(CHO)n where n is a real number.

Characteristics of carbohydrates.

1. They are either simple sugars or compound sugars.

The compound sugars are formed by condensation of simple `sugar molecules.

2. They are hydrate of carbon from the proportion of hydrogen and oxygen in water. 3.
The basic carbohydrate unit is thus a sugar which is the derivative of a poly hydrosol
alcohol.

• Alcohol is the paraffin compound with hydrogen atom replaced by the univalent hydroxyl
(OH) group.
• Paraffin is aliphatic or chain of compounds of carbon and hydrogen in which the carbon
atoms are linked by single bonds to adjacent atoms. (see Example above).
• The simpler hydroxyls are the glycol and glycerol and the simplest of sugar is the
glycerose (glycerin).

The carbohydrate contains several hydroxyl groups.

4. Some contain aldehyde (-CHO) group and others contain ketone group ( -CO-)

Examples;

1. Glucose: is a pentahydroxyl alcohol with the aldehyde group.

GLUCOSE
2. Fructose: is the pent hydroxyl alcohol with ketone group.

Complex sugars are built from the basic sugar units called monosaccharides through the
process of condensation polymerization.

Many sugars are reducing sugars and others are non-reducing sugars but give rise to
reducing sugars on hydrolysis with enzymes or mineral acid (mostly dilute HCL)

NB:Carbohydrates are called reducing sugar because they act as reducing agents
supplying electrons from their functional groups i.e. the aldehyde and ketone groups

which can reduce the cu2+ ions to cu+ions which appear orange or yellow ppt
(precipitate).
 The true carbohydrates are saccharides with a combination of sugar units. These are
divided into three main classes

1. monosaccharides – with a single sugar unit

2. Disaccharides – with two sugar units.
3. Polysaccharides- with many sugar units.

SUGAR

Sugar which include mono and disaccharides are all soluble in water. They have a sweet

taste. They are crystalline and small molecules.

Those with a potentially active aldehyde or ketone group are the reducing sugars e.g. glucose.

sugar Natural occurrence

Glucose Plant juice and grape sugar
Galactose From fruits.
 Fructose From fruits
Maltose From germinating seeds ( cereals) Sacrose From sugar cane ( in
plants)
Lactose From milk

Sugars without potentially active reducing groups are known as non-reducing sugars
e.g. Sucrose (C12H22O11).

Monosaccharides

• Have general formula (CnH2nOn)

• All are reducing sugars

• They are classified according to the number of carbon atoms e.g.;

Trioses have 3 carbon atoms

Tetraoses have 4 carbon atoms

Pentoses have 5 carbon atoms

Hexoses have 6 carbon atoms

Heptoses have 7 carbon atoms

-Of code, hexoses and pentoses are most common and triose being the true

sugar. -Pentose sugars are never occurring but only in combination with other

groups Of compounds.

Riboses- this occurs in one kind of nucleic acid. A derivative of deoxyribose

Hexose. The most important free sugar.

D-glucose

D- Fructose these are the most common sugars.

Structure of Monosaccharides

Glucose in common with other hexoses and pentoses easily forms stable ring structure. At any one time
most molecules oxists as rings rather than
In case of glucose carbon atom number 1 may combine with the oxygen atom an carbon 5. This form a six -
sided structure known as a pyranose ring
In case of fructose, carbon atom number 2 links with the oxygen an carbon atom number. This form a five
sided structure known as furanose ring Both glucose and fructose can exist in beth pyranose ring.

In case of fructose, carbon atom number 2 links with the oxygen on number 5. This form a five sides
structure known as furanose ring Both glucose and fructose can exist in both pyranose and furanose and
furanose ring form.

STRUCTURE PG 13 UB
Furanose

o Most carbohydrate in common glucose can exists as a numbee of isomers (they posses the same
molecular formula but differ in the arrangement of this atoms). one type of isomer called stereo
isomerism. occurs when the atom, or group, are joined together but differ in Their arrangement in
space one form of stereoisomer is called Optical Isomersm, result in isomer which can rotate the
plane of polarized light. If the substance rotates the plane of polarisation to the right it is said to be
dexTro-rotatory (d) and if to the left is laevo-rotatory (L) Optical isomerism is a property of any
compound which can exist in two forms whose structure are minor image. Like right and left handed
gloves

Example.
Stady the structure of glycerin (ghycer aldehyde)
L-Form isomer mirror. D-form isomer

Functions of monosaccharides.

1. PENTOSES (C5H10O5 ) e.g. ribose, deoxyribose, ribulose.

1. Synthesis of nucleic acids e.g. Ribose is the chief constituent of the RNA.
2. Synthesis of co-enzymes e.g. ribose synthesis (NAD and NADP)

HEXOSES (C6H12O6) e.g. fructose, glucose, galactose.

1. Sources of energy when oxidized by respiration.

2. Synthesis of disaccharides.
3. Synthesis of polysaccharides.

TRIOSES (C3H6O3) e.g. glyceraldehydes, dihydroxyacetone.

1. Intermediate in respiration (glycolysis).

2. Photosynthesis (dark reaction) RUBP as an acceptor of CO2
3. Carbohydrate metabolism.

Disaccharides

*Disaccharides are formed by the condensation or polymerlization of two

monosaccharides.

The most common disaccharides are;

1. Maltose = glucose + glucose

 2. Lactose = glucose + galactose
3. Sucrose = glucose + fructose.

In reducing sugars e.g. Lactose and maltose, one of the hexose residue retains its

aldehyde or ketone groups as an intact unit as reducing sugar.

Maltose is a disaccharide produced upon incomplete hydrolysis of the polysaccharide

starch. -It is found in germinating seeds.

-It is also produced commercially for use in production of beer.

-Maltose is produced of two D-glucose units joined by a α-glycosidic bond between the
anomeric carbon of one glucose unit and the number 4 carbon of the other glucose unit.

This specific bond formed an α-1,4-glycosidic bond also found in starch and glycogen.

NB: The numeric hydroxyl group of one of the glucose units participates in the glycosidic bond
and

Therefore cannot be easily oxidized.

However the anumeric hydroxyl of the other glucose unit is not as occupied and this glucose unit
exists in the equilibrium with free aldehyde solution.

Thus maltose is oxidized by Fehling’s solution, benedict’s solution or any other suitable

reagent.
Lactose

Constitutes some 3% to 5% of the milk of animal including cows and humans.

This disaccharide is composed of one galactose unit and one glucose unit joined by a glycosidic bond between the
anomer of galactose and the number 4 carbon of glucose. A β-1, 4 –glycosidic bond.

Glucose unit of the lactose still exists as an equilibrium mixture of α and β anomers

and the free aldehyde in solution. Lactose is thus a reducing sugar.

Sucrose

-It is found in fruits and vegetables.

-Sugarcane and sugar beets are the commercial sources and used as table

sugar. -Sucrose is composed of one fructose unit joined by two glycosidic

bonds.

Sucrose is not a reducing sugar since both anomeric carbons participates in the

glycosidic bonds and thus no free aldehyde or ketone exists in solution.

NB: D is the hydroxyl group attached to the anomeric carbon atom (the anomeric hydroxyl
group) is

drawn on the same side of the ring as the last -CH2OH group for the β-anomer and the opposite
side

of the ring for the α-anomer.

The D-galactose only differs from the D-glucose only in the orientation of the groups bonded to

Carbon no. 4. Ingested D-glucose (from milk and some other complex polysaccharide) is
normally

converted to D glucose in the human body.

The inability to perform this ionization (conversion of one isomer to another) results in a disease
called galactosemis.

POLYSACCHARIDES

-Have high molecular weight formed by condensation of large number of monosaccharide

units. They include;

 • Starch, glycogen, cellulose, chitin and insulin.

-All polysaccharides are insoluble in water forming colloidal solution.

-They are non –reducing sugars.

-They are Non- crystalline and as structural materials e.g. Cellulose.

-Represented by chemical formula ( C5H10O5) n or (C6H10O5)n where n is a whole number

ranging from 300-400.
 1. Starch

• Usually occur in a white powder-form at room temperature.

It forms a solution with hot water and a gel on cooling.

• During digestion, it is converted to a mixture of detrins. Later from maltose to glucose

units.
• It is largely stored in plants and it is a result of photosynthesis.
• In plants, starch is found in the storage parts such as roots and stem tubers, corn and some
rhizomes.

A starch granule is composed of

• A core of amylase
• Amylopeptin
• Amyloplast membrane.

Diagrams of amylase and amylopectin.

NB: Amylase and amylopectin are two different forms of starch.
• Both have linear chains of glucose units joined by α-1, 4-glycosidic bond.

Amylase is linear polymer of α-1, 4-glucose unit and is insoluble in water.

Amylopectin is a branched polymer; the main chain of amylopectin is joined by α-1,4-glycosidic

bond as in amylase. However about every 20-30 glucose units there are branches joined by α 1,6-
glycosidic bond.

Amylopectin is not soluble in water.

When boiled to about 2000C starch is partially hydrolyzed to a mixture of dextrins. However,
when heated with dilute mineral acids, starch is hydrolyzed via dextrin to glucose.

-In living things (tissues) the hydrolysis is of the following sequence.

-A suspension of glucose gives a blue black coloration with iodine.

-Amylopectin is compact as it has many branches of 1, 6- glycosidic bonds.

Biological importance

1. Storage of food in seeds, example; cereals and legumes

2. Important for human food.

GLYCOGEN

-This is called animal starch formed by condensation polymerization of glucose on

units. -It is very similar to amylopectin in structure.

-It is a polymer of glucose units joined by α-1,4- bonds and with α-1,6- bonded branches . it is a
white soluble powder and non reducing sugar.

OCCURRENCE

1. Mainly in vertebrates liver and muscles.

2. Also some maize seeds and fungi.

Glycogen differs from amylopectin because it is more highly branched than amylopectin
with one branch point about every 8 and 12 glucose units.

Biological advantage.

• It is important food storage in muscle and liver of vertebrates and fungi.

• It provides energy and is an energy substance.
 CELLULOSE

This is an important structural material in plants.

It largely constitutes the chemistry of the cell wall.

-Chemically cellulose is composed of several thousands of glucose units joined together

by 1, 4- glycosidic bonds. The units are so arranged that the bonds alternate in
appearance.

-This lead to the cross links of hydrogen bonds between the parallel running cellulose
molecules.

As a result of this, cellulose becomes tough with very high tensile strength.

The shape of a cellulose fibre is of the nature below.

Chemical structure of cellulose is presented as follows.

Hydrolysis of cellulose.

In the living tissues, hydrolysis of cellulose takes place in two stages;

Commercial use of cellulose

1. It is a raw material in the manufacture of many industrial products such as papers, rayon
and plastics.
2. The rayon made from cellulose are used in the manufacture of industrial belts and tyre
cords.
3. Cellulose derivatives such as cellulose nitrate are used in the manufacture of films.
4. Cotton, a pure form of cellulose is used in the manufacture of clothes.

CHITIN

This is closely related to cellulose in structure and function, being a structural polysaccharide.

-Structurally it is identical to cellulose except that the OH group at carbon 2 is replaced by

– NH.CO. NH3.

-This is a result of amino sugar (glucosamine) combine with acetyl group.

Chitin is therefore a polymer of N-acetylglucoamine.

Inulin

This is another storage carbohydrate which largely occurs of many plants.

It also occurs in small quantities in many monocots. Hydrolysis by dilute mineral acids or
specific enzymes e.g. inulin produce fructose only.

It is a polymer of fructose molecule.

Inulin inulase fructose

Summary roles of carbohydrates.

1. They built up a cell plasma membrane. It is made up of carbohydrates and so they are
used to build up the body of a living organism.
2. They are used as a substrate in respiration (to produce energy) as raw materials. Glucose
is the base raw material in glycolysis.

Are useful in pollination. Nectar which attracts pollinators is made up of sugars. Are

useful in storage purpose for future metabolism eg starch, glycogen and laminarin.

Used in the balance of osmotic pressure as they make solutes in the blood.

3. Are used in inheritance and control of the body activities as they make the genes e.g.
deoxyribose of DNA and ribose of RNA are pentose sugars.

*Other uses are from the above discussions.

LIPIDS

These are organic compound made up of elements carbon, hydrogen and oxygen in which its
proportion of oxygen is smaller than that of hydrogen (i.e. not in the ratio of carbon dioxide of
2:1)

Properties of lipids.

The features that characterize the lipids include the following;

1. They are either liquids or non-crystalline solids at room temperatures.

2. They are higher than water ( less dense than water)
3. They are hydrolyzed by alkaline into their respective constituent compounds. This
process is called saponification.
 4. They contain either saturated or unsaturated hydrocarbon chains.
5. In the presence of water and alcohol they form an emulsion.

*They are esters of higher aliphatic alcohols.

*all lipids are insoluble in water but soluble in organic compounds or solvents e.g. ether,
chloroform and hot alcohol.

They occur in adipose tissues of animals and some are a component of the protoplasm of all
living cells.

Lipids have ester linkage.

I.e.
Because of unsaturated bonds which are easy to break, that are why they are liquid at room
temperature, solids contain saturated bonds.

SIMPLE LIPIDS

Simple lipids are oils and fats of which are esters of glycerol. (Higher alcohol). Than glycerol
forms the ester called waxes.
-Oils and fats are formed by the combination of fatty acids and glycerol e.g. oleic acid which are
widely distributed in many fats and oils.

-They are also known as triglycerides.

Natural fats and oils.

They are a mixture of glycerides (esters) of fatty acids and glycerol.

Oils: contain greater proportion of unsaturated fatty acids; they are liquid at 200C.

Fats: contain a greater proportion of saturated fatty acids; they are solids at 200C.

BIOLOGICAL IMPORTANCE OF LIPIDS.

1. They form an insulation material thus prevent heat loss in organisms and animals
particularly.
2. Prevent water loss, form water proof in organisms, plants and insects.
3. Can be a stored form of energy in the body of an organism e.g. amoeba and seed like
units.
4. Form the basic constituent of the cell membrane as well as the cell components.eg
phospholipids
5. Enables large aquatic organisms like whales to have buoyancy.
6. Contains basic fat soluble vitamins A, B, D and K.
7. Forms the natural rubber.
8. It is a constituent of hormones like steroids e.g. oestrogen, progesterone, also acdysome
hormone in insects and crustacea are made up of lipids.
9. Gives more energy in metabolism.
10. Used to make bile salts (sodium taurochlorate and sodium glycochorate) for
emulsification in the duodenum.
11. Limits the linkage of small molecules across plasma membrane (cholesterol). 12.
Constituent of myelin sheath; helps to prevent outward flow of ions which would short
circuit the movement of ions along the nerve. Also enhance the salutatory condition.

PROTEINS

Proteins are nitrogenous compounds formed by condensation polymerization of larger

number of amino acids.

-Proteins are thus polymer molecules of amino acids.

Element present in proteins are carbon, hydrogen, oxygen, nitrogen, sulphur acid and
phosphorous and iron.

THE AMINO ACIDS

There are 20 amino acids which are polymerized to give many types of proteins.

Physical properties.

• They are colorless.

• They are Crystalline solid.
• Form colloidal solution.
• Coagulate on – heating

- Strong acid or base

- Presence of heavy metal

- Organic detergent.

• They are specific in nature of action.

Substances which are protein in nature are;

1. Albumin – egg albumin and serum albumin.

2. Histone – make the chromosome of nucleus.
3. Globular- blood fibrinogen, prothrombine and antibodies.
4. Schleroproteins- keratin (of hair and feathers) also keratin of skin, collagen which makes
tendon, bone, connective tissue myosin (muscles), silk (spiders web).

GENERAL PROPERTIES OF PROTEINS

1. They are polymers of amino acids.

Many are large dimmers with many amino acid units. Eg serum globulin of human blood
have 736 amino acids, myosin of muscle has 780 amino acids.

2. Colloidal in nature.
3. Amphoteric properties.
4. Every amino acid regardless of its side chain has an acidic carboxylic group and a basic
amino group or it has acid-base properties i.e. is said to be amphoteric.

-In solid state the amino acid have base salt like properties because they have both a
positive charge part and a negative charge part such substances are called zwitterions.

-Zwitterions are produced from the molecular form of the amino acid by internal-acid
base reaction.

NOTE: in the reaction above, neither the molecular form nor the zwitterions form has a
net electrical charge. In aqueous solution these two forms are in equilibrium but the
equilibrium overwhelmingly favors the zwitterions at any pH.

At any pH, some of the alamine in solution exists in the positive ion form. Some of it in
the negative ion form, some in the zwitterions form and some in molecular form.

• If the solution pH is very high that is ( H3O+) or (H+) is very low, both of the equilibrium
in the reaction is shifted to form the right and the negative ion form of alamine
predomination.
+ +
• On the other hand, if the solution pH is very low that is (H3O ) 0r (H ) is very high- both
equillibria in reaction above are shifted to the left and the positive form of alamine
predominates.
• At the pH of human cell and fluids (pH7) alanine exists primarily as the zwitterions.

In solution that are predominantly basic (i.e. pH btn 8.5 to 10.5), no single form of
alanine predominates. In this pH range, there are roughly comparable amount of
zwitterions and the negative charged.

• Similarly in moderately acidic solution there are roughly comparable amount of the
zwitterions and the positively charged form of alanine.
• The amount of positive or negative charge is affected by pH. Each molecule has a specific
pH which the total positive charge is exactly equally to the total negative charge. It is
electrically neutral and has no tendency to move to either the anode of cathodes of an
electric field. This is known as isoelectric point.

At higher pH protein and amino acid become more negative while at low pH they
become more positively charged.
 Properties of isoelectric point.

1. Solubility- have greater tendency to precipitate or coagulate.

2. Stability- as emulsion colloids.
3. Osmotic pressure- swelling by inhibition of water.
4. Viscosity and acid and base bonding properties.

5. They have large size molecule e.g. hemoglobin of mass 6000 and more. The enzyme
urease nearly 500,000.
6. Denaturation – there are easily denatured by heat, ultraviolent reactor and chemicals.
Denaturation alters the structure of proteins.

Structure of amino acids.

The amino acid consists of an α carbon surrounded by;

1. Hydrogen atom(H)
2. Amino group or amine group (-NH2), giving the nature of amino acid.
3. The carboxyl (-COOH) giving the acidic nature of amino acid.
4. The R-group known as the side chain. It presents the hydrogen atom or any other group
as alkyl group.

How peptide bonds are formed.

Proteins are polymers of amino acids joined together by peptide bond.

OTHER BONDS FOUND IN PROTEINS.

1. Ionic bonds: is an electrostatic attraction between positive and negative charge. 2.

Hydrogen bond: this occurs between hydrogen atom and more electronegative atoms. 3.
Disulphide bond: the bond between two crystalline molecules.
4. Van-de-Waal forces: these are weak non-attraction forces (hydrophobic interactions)
created between –CH3 groups which are non-polar.

CLASSIFICATION OF PROTEINS.

CRITERIA

1. Level of organization.
2. According to function.
3. According to composition.
4. To whether they contain essential amino acids.
5. According to structure.

ACCORDING TO LEVEL OR ORGANISATION.

1. Primary structure.
2. Secondary structure.
3. Tertiary structure.
4. Quaternary structure.

1. Primary structure.
This is a linear sequence of amino acids joined together by peptide bonds. Also
disulphide bond may be found.

2. Secondary structure

This is due to coiling or twisting of the polypeptide.

Diagram

α helical
 This is due to attraction of various amino acids. This is a component of hair, claws, nails,
as well as skin.

β pleated sheets (zig zag structures)

Collagen is a compound of tissues like bones and cartilage. Collagen is an example of β

pleated sheets.

3. Tertiary structure.

Tertiary structure is due to coiling and twisting of the polypeptide helix forming a
globular or spherical shape.

Bonds present in the coiled structure are ionic bond, hydrogen bonds, hydrophobic
interactions, disulphide bridges.

Examples of tertiary structures. (They are very soluble).

1. Immune globin( antibodies)

2. homornes
3. enzymes
4. Quaternary structure.

Quaternary structure is due to coiling and twisting of various polypeptide chains usually
the structure is associated with non-protein parts called prosthetic groups e.g.
hemoglobin.

Hemoglobin has four polypeptide chains, two α-chains and two β chains each
surrounding an iron atom.

The hemoglobin consists of protein parts. The protein part consist of 4 polypeptide
chains, of the four polypeptide chains, 2α chains and 2 β chains and is called
globin.
 The non protein parts is called HAEM consist of poiphyding surrounding an iron atom.

THE FOUR LEVELS OF PROTEIN STRUCTURE

1.
ii. BASED ON WHETHER THEY CONTAIN ESSENTIAL OR NON ESSENTIAL
AMINO ACIDS.

Essential amino acids Vs non essential amino acids

Essential amino acids are those which cannot be synthesized by human cells but are obtained
from food.

All of the 20 α amino acids are needed to make different proteins in the body of a human.

Twelve of these amino acids can be synthesized by the cells from other substances that are
present in the body; these are called non-essential amino acids.

The other eight cannot be synthesized by the body and must be included in the persons diet are
called essential amino acids.
 iii. BASED ON COMPOSITION.

1. Simple proteins

Simple proteins are made up of amino acids only.

E.g. - Histones (nucleoprotein)

• Globulin( immunoglobulin)
• Schleroproteins ( e.g. Keratin)
• Albumins
• Pastamins

1. Conjugated proteins.

Made up of amino acids; are globular proteins associated with non protein materials. E.g.
haemoglobin glycoprotein (components of cell membrane), mucin (component of saliva),
lipoproteins (components of cell membrane).

iv. ACCORDING TO FUNCTION.

NOTE:these are also functions proteins.

1. TYPE EXAMPLE OCCURRENCE/ FUNCTION.

Structural - Collagen - Components of the connective

tissue, bone, tendon,cartilage,
- Keratin skin,hair,feather, nails and horns.

- Elastic connective
tissues(ligaments ‘wraps up’
nucleic acid for virus.

-Elastin

-viral coat protein

2. Enzymes - Trypsin.

- Ribulose biphosphate
carboxylase.
 3. Hormones -Insulin

- glucagon

Adrenaline
corticotrophic hormone
(ACTH).
4. Respiratory - Haemoglobin
pigment.
- Glutamine
synthesase.
- Myoglobin
5. Transport - Serum albumin

6. Protective - Antibodies

- Fibrinogen

- Thrombin
7. Contractile - Myosin

- Actin
8. Storage - Ovalbumin

- Casein

- Catalyze hydrolysis of proteins

- Catalyses carboxylation (oxidation)CO2 of ribulase

biphosphate in photosynthesis.

- Catalyze synthesis of amino acids, glutamine from

glutamic acid and ammonia.

- Helps to regulate glucose metabolism.

- Stimulates growth and activity of the adrenal cortex. - Form fibrin in blood clotting

- Transports oxygen in - Involved in blood clotting mechanism.

vertebrate’s blood. - Moving filaments in myofibrils of muscles

- Stores O2 in muscles. - Stationary filaments in m myofibrils in muscles.

- Egg white protein
Transports fatty acids and lipids in the blood.
- Form complexes with foreign proteins - Milk proteins

- Enzymes
9.
Toxins- Snake venom
- Toxin made by diphtheria
- Diphtheria toxin
bacteria.

NEUTRAL AMINO ACIDS.

This is because their side chains have no charge at the pH of body cell.

Thus are divided into;-

• Natural hydrophobic amino acids.

• Natural hydrophilic amino acids.

Natural hydrophobic amino acids.

Seven natural amino acids have side chains(R) that are non polar or hydrophobic. These
hydrophobic are either alkyl or aromatic in nature.

• Alanine (ala).
• Valine (Val).
• Leusine (leu).
• Iso leusine.
• Proline
• Phenyl donine (phe)
• Tryptophan (trp).

Neutral hydrophilic amino acids.

 Eight amino acids are classified as hydrophilic.

• In general these amino acids are more soluble than hydrophobic amino acids. • The
acid chain of glycine (gly) is just hydrogen. The other seven neutral hydrophilic amino
acids have side chains that can form either strong or weak hydrogen bond with water.
• These have hydroxyl group in either side chain serine (ser) theorine (Thr) or tyrosine (try).
Two contain an amino functional group, asparagines (asp) and glutamine (gln). The
remaining two contain a sulphur atom cysterine (cys) and methionine (met).

Others include: tyrosine, asparagines, cysterine, glutamine, and methionine.

ACIDIC AMINO ACIDS

Acidic amino acids have side chains that contain a second carbonyl group.

At the pH of cells in the body, these carboxylic groups exist primarily as negative charged
carboxylate ions and this interact strongly with water molecules.

Aspartic acid (asp)

Glutamic acid (glu)

BASIC AMINO ACIDS.

Three of the amino acids contain a side chain that act as a proton acceptor or base. They are thus
classified as basic amino acids, these are lysine (lys), arginine (arg) and histamine.

v. BASED ON STRUCTURE

a. fibrous protein.

• Have a secondary structure and little or no tertiary structure.

• Insoluble in water.
• Physically tough.
• Form long polypeptide chain cross linked at intervals forming long fibres or sheets.

Functions of fibrous proteins.

Perform structural function in cell and organism e.g. collagen (tendon, bones, connective tissues)
myosin in muscles, (silk) spider web, keratin (nail, hair, feathers).

b. globular proteins.

• Found mostly in tertiary structure.

• Polypeptide chain highly folded to form spherical shape.

• Easily soluble in water.

Functions of globular proteins.

Forms enzymes, antibodies and some hormone e.g. insulin.

C. intermediate protein.

Fibrous in nature but soluble in water e.g. fibrinogen.

Function of intermediate protein.

Fibrinogen forms insoluble fibrin when blood clots.

NUCLEIC ACIDS.

Like proteins, nucleic acids are largely polymers made up of small number of different building
blocks called nucleotides.

Each nucleotide is in turn composed of 3 smaller parts.

- A phosphate group.

- Monosaccharide

- A nitrogen containing base.

 The term nucleotide is used to refer to nitrogenous base bound to a

monosaccharides. And the nucleotide is a nucleotide phosphate.

There are two major types of nucleic acids.

-i. deoxyribose nucleic acids (DNA).

-ii. ribonucleic acid (RNA).

Diagrams
There are two main differences between the deoxyribonucleotide components of DNA and the
ribonucleotide component of RNA.
criterion DNA RNA

- Has its sugar D-ribose lacking

1. Sugar - Has its sugar D-ribose
hydroxyl group in carbon #2 of
component having oxygen at carbon
ribose; hence the prefix De-oxy is
number 2.
used to denote the absence of
oxygen at that position.
- Have four possible
- Have four possible organic organic bases, 3 of which
2. Organic bases. bases, 3 of which are adenine, are adenine, guamine and
guamine and cytosine and the cytosine and the fourth
fourth is thymine which is lacking is uracil which is
in RNA. lacking in DNA.

JOINING THE NUCLEOTIDES TO FORM A POLYMER OF DNA OR RNA.

The bond that holds these polymers together are ester linkage formed between the phosphate on
the number 5 carbon of ribose in one nucleotide and the hydroxyl on the number 3 carbon of
ribose in the next nucleotide (deoxyribose in the case of DNA)

Two nucleic acids are said to have 3l5l- phosphate ester bridge/bond between their nucleotide
components

Diagram of a long nucleic acid.

 • The DNA consists of two long polynucleotide strands and the base components of each
nucleotide on one strong can form hydrogen bonds with only one specific nucleotide base
on the other strand.
• Guamine (G) can hydrogen bond only to cytosine in another DNA strands form a base
pair.
• Adenine (A) can hydrogen bond with thymine (T).

ATP (ADENINE TRIPHOSPHATE)

• ATP is formed from the nucleotide adenosine monophosphate by the addition of two
further phosphate molecules.

Its structure:

Diagram
 • ATP is an energy store, because the last branches are highly energetic on breaking. • The
hydrolysis of ATP to ADP is catalyzed by the enzyme ATPase and the removal of the
terminal phosphate yield 30.6kj mol-1 of free energy. So does the second one to from ADP
and AMP respectively. AMP and ADP may be re-converted to ATP by the addition of
phosphate molecule in a process called phosphorylation of which there two main forms.

1. Photosynthetic phosphorylation- occurring during photosynthesis in chlorophyll

containing cells.
2. Oxidative phosphorylation - occurring during cellular respiration in all aerobic cells.

USES OF ATP.

A metabolic active cell may require up to two million ATP molecules every second. ATP is the
source of energy for;

1. Anabolic processes.

It provides the energy needed to build up macromolecules from components

units. Examples

• Polysaccharide synthesis from monosaccharide.

• Protein synthesize from amino acids.
• DNA replication.

2. Movement- it provides the energy for many forms of cellular movements,

 including; -muscle contraction

- Cilliary actioning

- Spindle action in cell division.

3. Active transport – it provides the energy necessary to move materials against

concentration gradient e.g. ion pumps.

4. Secretion – it is secreted to form the vesicle in the secretions of the cell product.

5. Activation of chemicals – it makes chemicals more enabling them in reacting (more

readily) e.g. the phosphorylation of glucose at the start of glycolysis.

ENZYMES

• Enzymes are simple or compound organic proteins which are organic catalysts catalyzing
reactions in living tissues.

ENZYME: Greek word “en” means in and “zyme” means yeast cell.

They are bio catalysts found in living things.

• Catalysts accelerate chemical reactions although a catalyst is a participant in a reaction and

undergoes physical change during the reaction. It reverts to its original state when the
reaction is complete.
• Enzymes are protein catalysts for chemical reactions in biological systems. Most
chemical reactions of living cells would occur very slowly, were it not for catalyzing
enzymes as illustrated below.

Energy diagram under catalyst action showing progress of the reaction.

Fig. reduction of necessary activation energy by enzymes.

NB: as seen in the above graph, the activation energy (Ea) necessary to initiate the reaction is
much less in the presence of the catalyst than in its absence.

• It is this lowering of activation energy barrier by enzyme catalysts that makes possible
most of the chemical reactions in life.
+ -
• By contrast to non-protein catalyst (e.g. H , OH , or metal ions) each enzyme catalyze a
small number of reactions, frequently only one and thus enzymes are reaction –specific
catalysts.

• Most inorganic catalysts are relatively non specific for example platinum, often used to
catalyze the formation of water from hydrogen gas and oxygen gas. Will catalyze almost
any reaction in which H2 is one of the reactants and the reaction of materials as well.

Properties of enzymes.

1. They generally work fast than inorganic catalysts and greatly lower the activation energy.
2. Enzymes are not consumed by the reaction they catalyze i.e. a given molecule of an
enzyme can be used indefinitely if the conditions are kept suitable.
3. Enzymes can work in either direction i.e. catalyze reversible reactions. This is due to the
fact that metabolic reactions are reversible and the direction of the reaction depends on
 the relative amount of substrates and products present.
4. Enzymes are denatured by excess heat (temperature) by the virtue of their proteineous
nature.
5. Enzymes are sensitive to pH. Every enzyme has its own range of pH at which it functions
effectively.
6. Enzymes are specific in the action they catalyze. Normally a given enzyme will catalyze
only one reaction or one type of reaction.
7. Enzymes react in only small amount. A very small amount of catalyst will transfer in a
very large amount of reactants.
8. They are colloidal in nature and thus provide large surface area for reaction to take place.
9. Enzyme activity can be accelerated or inhibited. The accelerators are called activators
e.g. Cu, Zn, Co, Cl, Ca. while the inhibitors are for example DOT, Pb, and Hg etc.

NATURE AND MODES OF ENZYME ACTIVITY.

Hypothesis explains the nature and mode of enzyme activity.

1. The lock and key theory (hypothesis) by Fischer.

In the model the three dimensional configuration of the enzyme represented the lock (the
active title) into which particular substrate (key) will fit.

The active site presumes to be rigid.

2. The induced fit model by Koshland.

Originally little more than an attractive hypothesis, this model now has received
considerable experiment support.

An essential feature is the flexibility of the region of the active site. In this mode, the
substrate induce the conformation change in an enzyme just like the shape of a glove is
affected hand wearing.

MOLECULAR STRUCTURE OF ENZYMES.

Enzymes are either composed of;

1. Protein alone-simple enzymes.

2. Protein and other non-protein molecule( i.e. conjugated enzymes)

The protein part of an enzyme is called Apanzyme.

Non- protein part is called co-enzyme.

The protein part of an enzyme is made up of enzyme protein zymoprotein.

The two component (the apoenzyme and coenzymes) make up the active enzymes called
holloenzymes.

Holoenzymes= coenzyme + apoenzyme.

Prosthetic groups are usually metallic ions such as Co, Mg, Ni, Cu, Zn (mineral salt). This is also
a non-protein part, the well known co-enzyme are those which function as hydrogen carriers, in
oxidation-reduction in energy metabolism. For instance coenzyme NAD, NADP, Q, A.
Coenzyme A is involved in transfer of an acetyl group.

These are substances which increase the activity of the halo enzymes. Their absence may retard
the catalytic activity of the enzymes or preventing it from acting.

Activators are usually inorganic ions e.g. Ca2+ for thrombo kinase, Cl for ptyalin, Mg2+ for
phosphate.

Coenzymes and activators are needed by the enzymes for proper activities.

FACTORS AFFECTING ENZYMATIC ACTIVITY.

1. Over a limited range of temperature, the velocity of enzyme catalyzed reactions increase
as the temperature rises. The exact ratio by which the velocity change for a 100C
temperature rise is the Q10 or temperature coefficient.

The velocity of many biological reactions roughly doubles with a 100C rise in
temperature ( Q10 = 2) and is halved if the temperature is decreased by 100C. Many
physiological processes e.g. the rate of contraction of an exercised heart- consequently
exhibit Q10 of about 2.

When the rate of enzyme catalyzed reaction is measured at several temperature the result
shows in the figure below is typical. There is an optimal temperature which the reaction
is most rapid. Above this reaction the rate decrease sharply due to heat denaturation of
the enzyme and below this the energy content of enzymes is too low to make them
participate in their reaction.

Fig. enzymes activity as a function of temperature.

2. Although temperature sensitivity varies somewhat from one enzyme to another the curve
shown here may be taken as applying to an average enzyme.

Its activity rises steadily with temperature (approximately) doubling for each 10 0C
increase until thermal denaturation cause a sudden sharp decline, beginning between
400C and 450C. The enzyme because completely ineffective/ inactive at temperature
above 600C presumably because its three dimensional configuration has been severely
disrupted.

Denaturation of a protein enzyme by heat is the loss of it biological activity. This can be
done also by heat, acid or high salt concentration.

2. pH.

Moderate pH changes affect the ionic state of the enzyme and frequently that of the
substrate also.

When enzyme activity is measured as several pH values optimal activity is generally

observed between pH values of 5 and 9. However the few enzymes eg pepsin is active at
pH values well outside this range. The shape of pH activity curves is determined by the
following factors.