Biochemistry Reviewer for MIDTERM

Villareal, Myka, M. FA1-BSN1-2

MODULE #9

ENZYMES - complex organic compound w/c has the ability of speeding chemical
reactions w/out being themselves affected in the process.
- In the absence of enzymes, the reaction may hardly proceed at all, whereas in
its presence the rate can be increased up to 10⁷- fold.
The study of enzymes is known as ENZYMOLOGY.
It function as being biological catalysts.

A. PHYSICOCHEMICAL NATURE OF ENZYME:

1. All enzymes are protein in nature. Enzymes follow the physical and chemical nature
of protein.
a. simple protein
b. conjugated protein: prosthetic group ( non-protein in nature )

2. They are sensitive to any or all of the denaturing agents including changes of the pH
of the medium.
3. They are heat labile
4. The are water soluble
5 Colloids that are soluble in water (2 or more mixtures mix together but not chemically
combined).
6. Highly selective

B. CO-FACTORS
- Non-protein group in an enzyme (prosthetic group)
- Protein portion called APOENZYME
- Two portions combined together called HOLO-ENZYME

2 CO-FACTORS:
1. Co-enzyme - nonprotein organic compounds
● Co-factor - termed non-enzyme part of the of the Co-enzyme
Examples: FAD - Flavine Adenine Dinucleotide
NAD - Nicotinamide Adenine Dinucleotide (found in vitamins)
FMN - Flavine Mononucleotide

Biotin: involved in carbon dioxide fixation reactions and fatty acid synthesis
Vitamin B12 (cyanocobalamin): Coenzyme involved in the transfer of methyl groups
Vitamin E: Needed for cellular and macrocellular synthesis (Sunshine vitamins)
Vitamin K: Coenzyme used in electron transport (electron transport)
 2. Metal-ion activator - inorganic ions
Examples: Fl, Cr, Mn, Fe, Co Cu, I
*Metalloenzyme contains an apoezyme and a metal ion cofactor.

REACTIONS:
1. Co-enzyme + apoenzyme - holoenzyme
2. Metal ion activator+ apoenzyme - holoenzyme

Active site: the region or the enzyme that binds the substrate.
Coenzyme Must be Regenerated: chemically changed by the enzymatic reactions in w/c
the participate. In order to complete the catalytic, the enzyme must return to its original
interactions.

● First digit represent the class

● Second digit stands for the subclass
● Third digit is the sub-sub class or subgroup
● Fourth digit gives the number of the particular enzyme in the list
Example: EC 1.1.1.2 (Alcohol Dehydrogenase)

SIX MAJOR CLASSIFICATION OF ENZYMES

1. Oxidoreductases - catalyzing oxidoreduction between two substances.
2. Transferases - Catalyzing a transfer of group other than hydrogen.
3. Hydrolases - Cleave bond and add water / hydrolysis reaction
4. Lyases - Catalyzing removal of groups from substrate by other hydrolysis.
5. Isomerases - Interconvention of optic, geometric or positional isomers.
6. Ligases - Linkage of 2 compounds coupled to the breaking of a pyrophosphate bonf
in ATP.
*Ligase is also known as synthetase
Synthetase - are ATP dependent enzymes catalyzing biosynthetic reactions.
Synthases - enzymes catalyzing biosynthetic reactions.

CLASSIFICATION OF ENZYMES ACCORDING TO CHEMICAL REACTION CATALYZED:

I. ADDITION OF WATER MOLECULES
A. HYDROLASE
a. Carbohydrase - aid in the hydrolysis of carbohydrates
b. Esterases - aid in the hydrolysis of esters
c. Nucleases - aid in the hydrolysis of nucleic acids
d. Amidases - aid in hydrolysis of amides
e. Proteases - aid in the hydrolysis of proteins
f. Peptidases - hydrolyze peptides to simple peptides and amino acids
II. TRANSFER OF ELECTRONS
A. OXIDASES - are enzymes which catalyze the removal of hydrogen from a substrate
and pass it directly to oxygen.
a. Dehydrogenases - active H atoms of organic compounds
b. Catalase - acts on hydrogen peroxide to give water and oxygen
c. Peroxidases - act on organic peroxides giving nascent oxygen
 d. Tyrosinase - acts on tyrosine
e. Ascorbic acid oxidase - acts on ascorbic acid
III. SPLITTING OR FORMING A C-C BOND
A. DESMOLASES - catalyze the linkage not broken by water; splitting or forming a C-C
BOND
a. Decarboxylases - i. carboxylase - alpha keto acids to CO2 and aldehydes, ii.
carbonic and anhydrase - carbonic acid to water and carbon dioxide
IV. TRANSFER OF A RADICAL
A. TRANSAMINASES - catalyze the transfer of amino acids group from amino acids
ketoacids.
a. alanine transaminase - the transfer of an alpha-amino group from an amino
acid.
b. glutamine transaminase - alpha-amino group from an amino acid to
alpha-ketoglutyaric acid to produce an alpha-keto and glutamic acid.

MODULE #10
ENZYMES (Commercial, Pharmaceutical, and Medicinal Enzymes)

SOME ENZYMES WITH THEIR SOURCES AND USES (Commercial, Pharmaceutical,

and Medicinal)

1. PROTEOLYTIC ENZYMES
a. Pepsin - digestive aid in pre-cooked foods, found in gastric juice
b. Alcalase - additive to remove protein stains
c. Bromelains - mixture of protein-digesting & milk clotting enzymes from the
juice of Ananas comosus, Fam. Bromeliaceae, meat tenderizer
d. Papain - obtained from the latex of Carica papaya, Caricaceae
Use: Relieve symptoms of episiotomy - cleaning solutions of soft contact
lenses.
Chymopapain - nonpyrogenic proteolytic enzyme obtained from the latex of
Carica papaya.
e. Trypsin - Secreted by pancreas - released in the intestines - active in an
alkaline environment. Chymotrypsin - crystalized from an extract of the
pancreatic gland of Ox (Bos Taurus, Fam Bovidae).
f. Sutilains - from Ba illusion subtilis, use of wound debridement
g. Rennin - enzyme that is present in the mucous membrane of the stomach pf
animals; For cheese making.
h. Erepsin - found in intestinal juice
i. Streptokinase - supplied as lyophilized powder; acts to covert plasminogen
to plasmin: use to treat pulmonary embolism
j. Urokinase - from human urine / obtained from human kidney cells.
k. Fibrinolysin - prepared commercially by activating a human blood plasma
fraction with streptokinase.
2. OXIDIZING ENZYMES
i. Peroxidase - widely distributed in plants: bring out the oxidation reactions that cause
discoloration of bruised fruits.
ii. Thrombin - converts the fibrinogen of the circulating blood into the insoluble fibrin of the
blood clot.

3. CARBOHYDRASE / AMYLOLYTIC ENZYMES

a. Amylase - found in the salivary glands; digestive aid in pre-cooked foods.
b. Diastase - yellowish white, amorphous powder obtained from an infusion of malt.
c. Amylopsin - found in digestive tract of animals; sometimes called "animal diastase"
d. Invertase or sucrase - found in yeast and in the intestinal juice: prevention of
granulation of sugar in soft-centered candies.
e. Zymase - fermenting enzyme causing the conversion of monosaccharides (glucose,
fructose) into alcohol and CO2.
f. Emulsin - found in almonds
g. Myrosin - found in white and black mustard
h. Amyloglucoside - production of dextrose from starch
i. Cellulase - preparation of coffee liquid concentrate
j. Lactase - prevention of lactose crystals concentrate
k. Pectinase - clarification of wines and juices
l. Hyaluronidase - occurs in human testes, in various bacterial cultures as a metabolic
product in heads of leeches and in snake venoms.

4. ESTERASES
a. Lipase - flavor production of cheese; found in pancreatic juice of animals and oily
seeds.
b. Pectase - splits pectin into pectic acid and methyl alcohol
c. Steapsin - lipolytic enzyme capable of digesting dietary fat
d. Urease - obtained from soybeans; use as a laboratory reagent for converting urea to
ammonia.

5. OTHERS
a. Collagenase - used in topically to debride dermal ulcers and severely burned areas
b. L - Asparagine - enzyme obtained from cultures of certain stains of Escherichia coli
c. Lypoxygenase - bread whitening
MODULE #11
ENZYMES (Mechanism, and Factors Influencing of Enzymatic
Action, Clinical Enzymology)

MODE OF ENZYME ACTION:

1. The surface of the substrate contacts a specific region of the surface of the enzyme
molecule called ACTIVE SITES.
*Activation Energy - minimum amount of energy that is required to activate atoms or
molecules to a condition w/c they can undergo chemical transformation or physical transport.

THEORIES EXPLAINING THE MODE OR ENZYME ACTION

I. FISCHER'S LOCK AND KEY THEORY - active site of the enzyme & substrate have
complementary structures, hence they fir together as a key fits a lock.

II. KOSHLAND'S INDUCED FIT THEORY - the substrate still needs to fit into the
enzyme like a key.

⬆️ ⬆️
FACTORS THAT INFLUENCE ENZYME ACTION:

⬆️ ⬆️
1. Concentration of substrate - concentration of substrate = enzyme action
2. " of enzyme - " enzyme = ""
3. Temperature - optimum temp of enzyme in the body = 37°
4. pH - each enzyme has its specific optimum pH at w/c it exerts its maximum activity.
Eg. Pepsin - 1.5 to 2.2 , Lactase - 5.7 , Trypsin - 7.8
5. Presence of accelerators - activate the enzymes
6. Presence of inhibitors - have the ability to combine w/ enzyme in a reversible
reaction & hence block enzyme catalysis.
7. Environmental hazards
A. Hg (mercury) - Hg from phenyl mercuric acetate -> to prevent cellulose from
rotting.
B. Methyl mercuric acetate - prevent rotting seed grains
C. Cd (cadmium) - derived from cigarette smoke; 1 pack = 15 mcg
D. Pb (lead) - present in gasoline; yellow-painted pencils.

MODULE #12
NUCLEIC ACID (Nucleic Acid Structures and Organization)

NUCLEIC ACIDS
● Consist of long-chained nucleotides (polynucleotides) combined w/ another thru
PHOSPHATE DIESTER LINKAGE
● Nucleotides linked by 3', 5' phosphodiester bonds
BIOLOGICAL SIGNIFICANCE:
1. Responsible for storage and transmission of genetic information code.
2. Precise synthesis of proteins characteristics of individual cell.

PROPERTIES OF NUCLEIC ACIDS:

1. Insoluble in alcohol
2. Slightly soluble in cold water but readily dissolved in hot water.

2 TYPES OF NUCLEIC ACIDS:

1. RNA - Ribonucleic acid (responsible for using the genetic information encoded in
DNA to produce thousands proteins found in living organisms).
2. DNA - Deoxyribonucleic acid (the nucleic acid that stores genetic information)

DNA - DEOXYRIBONUCLEIC ACID

- molecules of heredity
- made up of mononucleosides d-AMP; d-GMP; d-TMP linked in various sequence
with 3'-'5 phosphate diester linkage.
- base sequence
- backbone: P-sugar-P-sugar

DNA TYPES
● A-DNA: right handed double helix similar to the B-DNA form.
● B-DNA: the most common DNA conformation and is a right - handed helix.
● Z-DNA: Z-DNA is a left-handed DNA where the double helix winds to the left in a
zig-zag pattern. It was discovered by Andres Wang and Alexander Rich.
Eg. Pyramidine - C,U,T = PuyCU; Purine - A,G,A = PurGA

WHO DISCOVERED DNA?

- DNA was first recognized and identified by the Swiss biologist, Johannes Friedrich
Miescher in 1869 during his research on white blood cells.
- The double helix structure of a DNA molecule was later discovered through the
experimental data by James Watson and Francis Crick.

CHARGAFF'S RULE
● Erwin Chargaff - a biochemist, discovered that the number of nitrogenous bases in
the water was present in equal quantities.
A= T; C=G
● In other words, the DNA of any cell from any organism should have a 1:1 ratio
of purine and pyrimidine bases.
FUNCTIONS:
1. To make exact copies of itself in the process of replication
2. To transfer the genetic information to m-RNA in the process of transcription
● GENOME - DNA that constitute the total genetic information content of an organism,
the segments of the genome that can be translated is called GENE.
- Introns - DNA segment that do not convey code for genetic information
- Exons - DNA segments that convey genetic information
 × ALPHA -> HELIX -> WATSON -> CRICK MODEL
RNA - RIBONUCLEIC ACID:
- Single chain of nucleotides
- Made up of major Mononucleotides: AMP, GMP, UMP, CMP

3 FORMS OF RNA:
1. Messenger RNA (mRNA)
- made in the nucleus of the cell as a component to a DNA strand
- Pairing nile: UA, GC
FUNCTION: Serves as cytoplasmic messenger of genes
2. Ribosomal RNA (rRNA)
- Comprise 70-80% of the total cell RNA (most abundant)
FUNCTION: bind the m-RNA and a specific enzyme for protein synthesis
3. Transfer RNA (tRNA)
- 10-15% of the total RNA content of the cell (second most abundant)
FUNCTION: Carry specific amino acids to the ribosomes and decodes the genetic
information in mRNA in terms of proper amino acid sequence.

COMPOSITION OF NUCLEIC ACIDS:

● Nucleic acids are substances with high molecular weight ranging from 1286 to
3,000,000
● Made up of carbon, hydrogen, oxygen, nitrogen and phosphorus
● Nitrogen is from 15-16%, while phosphorus is from 9-10%

1. N-base:
Pyramidine
● Isolated from the hydrolysates of nucleic acid
● Pyrimidine bases have only one ring
● Pyrimidine derivatives such as:
- Vitamin B1 (Thiamine) - plays important role in metabolic processes
- Alloxan (2,4,5,6- tetraoxypyrimidine) produces experimental diabetes
and has natural diabetes mellitus
- Thiouracil / Propylthiouracil - used as antithyroid drugs
Purine
● made up of six membered pyrimidine ring and a five membered imidazole ring
(two rings)
- Uric acid -> weak acidic property
- Hypoxanthine
- Xanthine -> Caffeine (1,3,7 -trimthylxanthine) from tea and coffee
NUCLEOSIDES
● Are derivatives of purines and pyrimidines that have a sugar linked to a ring nitrogen
of a purine or pyrimidine

COMMON NUCLEOSIDES OF RNA:

A. Pyrimidine:
1. Cytidine = (Cytosine + Ribose)
2. Uridine = (Uracil + Ribose)
B. Purine:
1. Adenosine = (Adenine+ Ribose)
2. Guanosine = (Guanine + Ribose)

COMMON NUCLEOSIDES OF DNA:

A. Pyrimidine:
1. Deoxycytidine = (Cytosine + Deoxyribose)
2. Deoxyuridine = (Uracil + Deoxyribose)
B. Purine:
3. Deoxyadenosine = (Adenine + Deoxyribose)
4. Deoxyguanosine = (Guanine + Deoxyribose)

NUCLEOTIDES
● Functional subunits of nucleic acids
● Formed when 1 or more phosphate groups is attached to the 5'carbon of a nucleotide

MODULE #13
NUCLEIC ACID (Central Dogma)

THE CENTRAL DOGMA

- A series of theories of the transmission of heredity information and protein synthesis
- REGULATION OF PROTEIN SYNTHESIS: this is the concept that regulate cellular
activities.

● Francis Crick in 1956, when he first proposed that the sequence of nucleotides in
DNA determines the sequence of amino acids in a protein.
● Gene Expression - process by which the genetic code - the nucleotides sequence -
or a gene is used to direct protein synthesis & produce the structures of the cell.
REPLICATION DNA TO DNA
- a copying process by which DNA is applied to the new cells formed by cell division;
this genetic information is transferred to mRNA through transcription.
TRANSCRIPTION DNA TO RNA
- process involves the transfer of genetic info from DNA strand thru base pairing to
form complementary ribonucleotides, an RNA chain.
TRANSLATION RNA TO PROTEINS
- RNA to PROTEIN

3 REACTIONS:
1. Replication - patient DNA to daughter DNA
2. Transcription - DNA to messenger RNA
3. Translation - mRNA to CHON'S (reading is from 5' to 3')
● SEME-CONSERVATIVE REPLICATION - only 1 strand will undergo
transcription.

DNA TRANSCRIPTION
- is the synthesis or a complementary strand of RNA from DNA template.
INHIBITORS OF RNA SYNTHESIS
- Quinolones and Fluoroquinolones: inhibit DNA gyrase (prokaryotic topoisomeras II)
3 STEPS OF TRANSCRIPTION
1. INITIATION - the beginning of transcription.
2. ELONGATION - the addition of nucleotides to mRNA strand.
3. TERMINATION - the ending of transcription

DNA TRANSLATION
- codons of an mRNA are "read" sequentially
- Anticodon sequence of three basis that is complementary to a codon.
INHIBITORS OF PROTEIN SYNTHESIS
1. Reversible inhibitors in Bacteria (Bacteriostatic Agents)
a. Tetracycline
b. Chloramphenicol
c. Erythromycin
d. Clindamycin
2. Irreversible inhibitors in Bacteria (Bacteriostatic Agents)
a. Streptomycin

IMPORTANT ENZYMES IN CENTRAL DOGMA

1. DNA GYRASE relaxes supercoiling ahead of the replication fork
2. DNA LIGASE makes covalent bonds to join DNA strand
3. DNA POLYMERASE synthesize DNA; proofhead and facilitate repair DNA
4. HELICASE unwinds double-stranded DNA
5. PRIMASE RNA polymerase that makes RNA primers from a DNA template
6. RNA POLYMERASE copies RNA from an DNA template
MUTATION any chemical or physical change that alters the sequence of bases in the DNA
molecule.

MUTAGENS substance that causes mutation either physical or chemical form.

TYPES OF MUTATIONS:
1. SILENT MUTATION substitution occurs in the third position of the codon .
2. MISSENSE MUTATION change in one DNA base pair that results in the substitution
of one amino acids for another.
3. NONSENSE MUTATION also a change in one DNA base pair.
4. FRAMESHIFT MUTATION occurs when the addition or loss of DNA bases changes a
gene's reading frame.

GENETIC CODE set of rules which give a relationship between the nitrogenous bases & the
amino acids in a polypeptide chain.

BASIC PRINCIPLES OF HEREDITY:

TERMINOLOGIES
● ALLELES may replace one another at the same locus.
● HOMOZYGOUS when both alleles carry the same defect
● HETEROZYGOUS when one allele is normal, and the counterpart is defective
● PHENOTYPE observed character expressed by the gene
● GENOTYPE represents the set pattern of genes present in the cell.

AUTOSOMAL DOMINANT INHERITANCE only one copy of a disease allele

AUTOSOMAL RECESSIVE INHERITANCE two copies of a disease allele
SEX-LINKED (X-LINKED) RECESSIVE INHERITANCE disease occurs in both sexes w/
equal frequency.

FOUR CHROMOSOMAL ABNORMALITIES

1. TURNER SYNDROME alters development in females. This condition tend to be
shorter than average. Includes extra skin on the neck (webbed neck)
2. KLINEFELTER SYNDROME also known as the XXY condition
3. DOWN SYNDROME/ TRISOMY 21 genetic disorder & the most common autosomal
chromosome abnormality in humans.
4. CRI DU CHAT OR CRY OF THE CAT SYNDROME (CdCS or 5p-) is a rare genetic
disorder in w/c a variable portion of the short arm or chromosomes 5 is missing.
MODULE #14
CARBOHYDRATES

CARBOHYDRATES term carbohydrate originally referred to "hydrates of carbon" because

the general formula of these compounds was CnH2nOn or Cn(H2O)n.
SACCHARIDES building blocks / fundamental sub-units of carbohydrates
STORAGE FORM OF CARBOHYDRATE
- GLYCOGEN storage form of carbohydrate in animal tissue w/c is found in liver &
muscle m
- STARCH storage form of carbohydrate in plant tissue
BIOLOGICAL SIGNIFICANCE:
1. Carbohydrates are the main source of energy in the form of ATP
Metabolism process of breaking down into simplest forms

CLASSIFICATION OF CARBOHYDRATES:
a. Simple sugar / monosaccharides
b. Oligosaccharides
c. Polysaccharides
SIMPLE SUGARS / MONOSACCHARIDES these ar CHO's that cannot be hydrolyzed to
simplest forms.
I. According to functional group presents
1. Aldose - presence of aldehyde group
2. Ketose - presence of ketone group
II. Based on the no. of C- atoms in the molecule
a. Triose (C3H6O3) not found in free in nature but as products of carbohydrates
metabolism.
● glyceraldehydes or glycerose (Aldose)
● dihydroxyacetone (ketose)
b. Tetroses 4-C monosaccharides (C4H8O4)
● Erythrose (aldose)
● Threose (aldose)
● Erythrulose (ketose)
c. Pentoses 5-C monosaccharides
● Ribose - constituent of RNA
● Arabinose - present in cherries and can be seen in the body
● Xylose - seen in proteoglycans
● Lyxose - occurs rarely in nature
● Xylulose - an intermediate in uronic acid pathway
d. Hexoses 6-C monosaccharides, the most important monosaccharides found in
plants.
● Allose
● Altrose
● Glucose
● Mannose
● Gulose
 ● Idos
● Galactose
● Talose
● Fructose (ketohexose)
e. Heptoses 7-C sugar form a vital importance in the glucose metabolism of animals &
in the photosynthesis process of plants.
f. Octose 8- carbon sugar isolated from avocado pulp - D - glycerol - D - manno
octulose

OLIGOSACCHARIDES carbohydrates w/c on hydrolysis will yield 2-10 units

Disaccharides (C12H22O11) considered as the most abundant oligosaccharides
1. Reducing disaccharides those which contain a free aldehyde or ketone group
a. Lactose
● milk sugar least soluble and least sweet of all sugars
● B-D galactose + B-D glucose
● cow's milk -> 4-5 % lactose
● human 7-8% lactose
b. Maltose malt sugar found in germinating grains & in malt
● B-D glucose + B-D glucose
c. Cellobiose obtained from the hydrolysis of cellulose from wood & cotton
● B-D glucopyranose + B-D glucopyranose

Test for Reducing Sugar: (+) result

1. Barfoed's test brick red ppt
2. Benedict's test brick red ppt
3. Nylander's test black ppt
4. Fehling's test brick red ppt
Fehling's test clinical determination of glucose in blood or urine

Detection of Reducing Sugar in:

1. Fischer Formula free aldehyde or ketone group in the structure
2. Haworth Structure presence of an OH group at C1 (aldose) or C2 (ketose)
Non-reducing sugars: those whose aldehyde groups are involved in the linkage
a. Disaccharides
Sucrose a.k.a table sugar, cane sugar, saccharose, beet sugar (invert sugar is
sweeter than sucrose)
b. Trisaccharides C18H32O16
✓ Raffinose
● forms in sugar beets
● made up of glucose, fructose, galactose
c. Tetrasaccharides yield for monosaccharides molecules on hydrolysis
Starchyose - fructose + glucose + 2 molecules of galactose
POLYSACCHARIDES carbohydrates w/c on hydrolysis will yield several monosaccharides
units; more complex, high occular weight.
I. CELLULOSE GROUP:
CELLULOSE
● most abundant organic compound making up about 50% or more of the carbon
vegetation
● the purest source is cotton
✓ Pentosans (C5H8O4)n - xH2O - long chained of pentose units
1. Xylans found in wood, straw, rice bran and corn cobs
2. Arabans found in gum Arabic, mucilage & fruit juices
✓ Hexoxans (C6H10O3)n -x H2O
1. Glucosan starch yielding glucose
2. Agar agar
Dextran polysaccharides produced by certain microorganisms when grown on sugar media
✓ Hexopentosans
1. Pectins
● colloidal carbohydrates
● responsible for jellying properties of fruits
● commercially prepared from apples & lemons

MODULE #15
CARBOHYDRATES

HETEROPOLYSACCHARIDES:
● Polysaccharides w/c on hydrolysis yield mixtures of heteropolysaccharides & derived
products
● 2 MAIN GROUPS:
a. Neutral mucopolysaccharides
● made up of N-acetyl-hexosamine & hexose
b. Acid mucopolysaccharides
● contain hexuronic acid, sulfate or phosphate
HYALURONIC
● serves as a cementing substance in the tissues w/c allows the passage only of the
metabolites but not the infecting microorganisms.
HEPARINE (heparin)
● important acid mucopolysaccharide secreted by the lung tissues & certain types of
cells lining the arterial blood vessels.

FIVE GLYCOSAMINOGLYCANS (GAG) / MUCOPOLYSACCHARIDES

● HYALURONIC ACID serves as a lubricant & shock absorbent in joints
● CHONDROITIN is the most abundant GAG in the body; present in cartilages,
tendons, ligaments, and aorta which helps to maintain their shapes.
● KERATAN SULFATE only GAG w/ no uronic acid; found in cornea and tendon
- 2 types: keratan sulfate I - found in cornea, keratan sulfate II - found in
skeletal muscle
DERMATAN SULFATE found in skin, blood vessels, heart valves & cornea; maintains
overall shape of the eye.
HEPARIN the only intracellular GAG; an anticoagulant

PROPERTIES OF CARBOHYDRATES:
I. PHYSICAL
a. Monosaccharides & Oligosaccharides:
1. white crystalline solids
2. soluble in water
3. optically active
4. sweet taste
b. Polysaccharides are:
1. amorphous solid
2. low molecular weight form a colloidal dispersion in H2O
3. not sweet / no flavor at all
II. CHEMICAL
a. Hydrolysis
1. Disaccharides: C6H12O11 + H2OC6H12O6 + C6H12O6
2. Starch Hydrolysis
Starch -> amylodextrin->erythrodextrin->achrodextrin->maltose->glucose
Agents of Hydrolysis:
1. Heat
2. Acid
3. Bases
4. Enzymes
b. Reducing Property or Action of Carbohydrates:
● attributed to a free aldehyde or ketone group
c. Fermentation complex process which involves the breaking down of complex
substances with the aid of biological catalysts called ENZYMES
d. Osazone Formation (+) result: yellow crystals or yellow ppt.

Osazone Formation aids in the identification by:

a. each osazone has a definite crystals formation
● Maltose - petal-shaped
● Lactose - powder puff-shaped
● Galactose - rhombic-plate
● Glucose, Fructose, and Maltose - broom shaped
b. each has definite melting point.
3 Reactions Involved in Osazone Formation:
a. Formation of glucosazone
b. Formation of fructosazone
c. Formation of mannosazone
● Mannose first one to form an osazone
E. Molisch Test general test for carbohydrates except trioses & tetroses which lack the
minimum requisite of 5C atoms
- (+) Result: Violet ring at the junction
MODULE #16
CARBOHYDRATES (Glucose Transporter, Glycogen Storage
Disease, Carbohydrates Deficiency, and Sugar Substitutes)

GLUCOSE TRANSPORTER a facilitative protein involved in glucose translocation across

the cell membrane.
GLUT 1 location: Rbc, Colon, Brain, Kidney, Placenta (responsible for setting up the bssal
rate of glucose uptake
GLUT 2 loc: small intestine, kidney, islet of langerhans, liver (low affinity transporter)
GLUT 3 loc: placenta, neurons, kidney (high-affinity transporter)
GLUT 4 loc: heart, adipose tissue, skeletal muscle (insulin-stimulated glucose transport)
GLUT 5 loc: small intestine, testis, sperm (high affinity fructose transporter. Responsible for
shuttling fructose monosaccharides into the cells.
GLUT 7 loc: Liver (mediates glucose release from endoplasmic reticulum coupled to
glucose-6-phosphate.

GLYCOGEN STORAGE DISEASES

- also known as glycogenosis or dextrinosis
- a rare condition that changes the way the body uses and stores glycogen, a form of
sugar or glucose.
TWO FORMS
A. liver forms (type I,III, IV, and VI)
● marked by hepatomegaly due to increased liver glycogen and hypoglycemia
caused by inability to convert glycogen to glucose.
B. muscle forms (type II, IIIA, V, and VII)
● have mild symptoms appearing during stermous exercise owing to inability to
provide for muscle contraction.

Type I Von Gierke Disease (Liver, Kidney) Massive enlargement of the liver, severe
hypoglycemia, ketosis, hyperuricemia, hyperlipidemia.

Type II Pompe (All Organs) Cardiorespiratory failure causes death usually before age 2.

Type III Cori Forbes (Muscle & Liver) Like type 1 but milder course.

Type IV Anderson (Liver & Spleen) Progressive cirrhosis of the liver.

Type V McArdle (Muscle) Limited ability to perform strenuous exercise because of painful
muscle cramps.

Type VI Hers (Liver) Like type 1 but milder course

Type VII Taruis (Muscle) Like type V.

Type VIII Phosphorylase kinase (Liver) Mild liver enlargement. Mild hypoglycemia.
CARBOHYDRATE DEFICIENCIES:
1. MARASMUS CHO deficiency (shrinking)
2. DIABETES MELLITUS metabolic disease due to an absolute or relative deficiency of
insulin leading to changes in CHO, CHON & lipid metabolism
Insulin hormone resent or secreted by B-cells of Islets of Langerhans of the
Pancreas
2 TYPES OF DIABETES MELLITUS:
1. JUVENILE onset or Insulin Dependent Diabetes Mellitus (IDDM)
● common in adolescent as a result of high viral infection
● usually thin (underweight)
2. ADULT onset or Non-Insulin Dependent Diabetes Mellitus (NIDDM)
● occurs during late 20's or early 30's
● Heredity
4 P's of Diabetes Mellitus:
1. Polydipsia frequency of thirst
2. Polyuria frequency or urination
3. Polyphagia frequency of eating and hunger sensation
4. Persistence of non-healing wound
3 Pathies of DM:
1. Neuropathy involvement of nerve functions esp. sensory
2. Nephropathy involvement of the kidneys
3. Retinopathy involvement of the retina of the eye w/c might lead to blindness
2 Common Laboratory Findings in DM:
1. Glycosuria excessive glucose in urine
2. Hyperglycemia excessive in the bloodstream
COMMON SUGAR SUBSTITUTES:
1. ASPARTAME made up from aspartic acid & phenylalanine, both amino acids
● 200 times sweeter than sugar, not suitable for people w/ phenylketonuria
2. SACCHARIN is made from anthranilic acid.
● 300 times sweeter than sugar
● used in sweeten products such as, drinks, candies, med, & toothpaste
3. Erythritol a natural sugar alcohol
● occurs naturally in fruits & fermented foods
● 60-70% as sweet as table sugar yet it is almost non-caloric
4. Xylitol found in fibers of many fruits and vegetables
● roughly sweet as sucrose w/ only ⅔ the food energy
● a safe sweetener for people w/ diabetes that would not impact insulin levels.