BIOCHEMISTRY

By
SAHADEV PARMAR
Sahadevparmar_22@yahoo.com

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 AMINO ACIDS AND PROTEINS

- e

Imidazole grp

Indole - Tryptophan

Phenolic grp - Tyrosine

Guanidino grp Arginine

Amide grp - Asparagine & Glutamine

Hydroxyl grp - Serine &Threonine

Thio grp /sulfhydryl - Cysteine

Thio ether - Methionine

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Twenty kinds of side chains varying in size, shape, charge, hydrogen-bonding capacity, hydrophobic
character, and chemical reactivity are commonly found in proteins.

Cysteine is readily oxidized to form a covalently linked dimeric amino acid called cystine, in which two
cysteine molecules or residues are joined by a disulfide bond.
Histidine has an imidazole group. Histidine is the only common amino acid having an ionizable side
chain with a pKa near neutrality. It can be neutral or positive charged at pH 7. In many enzyme-
catalyzed reactions, a His residue facilitates the reaction by serving as a proton donor/acceptor.
Tryptophan (tyrosine and phenyl alanine are less) are aromatic amino acid which give a characteristic
strong absorbance of light at a wavelength of 280 nm, while nucleic acid and its bases are absorbs at 280
nm. a property exploited by researchers in the characterization of proteins and nucleic acid. The
metabolism of phenylalanine and tyrosine plays an important role in the biosynthesis of neurotransmitter
adrenaline and noradrenaline. while Tryptophan metabolism give serotonin neurotransmitter. Tryptophan
is the only amino acid which is fluorescent.
Proline has aliphatic side chain with a distinctive cyclic structure. The secondary amino (imino) group of
proline residues is held in a rigid conformation that reduces the structural flexibility of polypeptide
regions containing proline. Proline does not give ninhydrin reaction as this reagent reqiues free alpha
amino grp (-NH2) but proline have imino grp (-NH).
Glycine is the only amino acid which doesnot contain chiral center.
Isoleucine and threonine has two chiral centers.

O O
O H - H2O
O
O H H2 O
O O
Ninhydrin Indan-1,2,3-trione

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 O O

C N C

O O
Positive Test

For the amino acids which have free NH2 (amino) grp, ninhydrin test is positive but it is negative for proline
because it have only NH grp (Imino)

STRUCTURE OF PROTEINS

Primary Structure of proteins is a linear sequence in which amino acids are linked by Peptide Bonds to
Form Polypeptide Chains. Proteins are linear polymers formed by linking the alpha -carboxyl group of one amino
acid to the alpha -amino group of another amino acid with a peptide bond (also called an amide bond). The
formation of a dipeptide from two amino acids is accompanied by the loss of a water molecule. Primary structure
also includes disulfide bonds, formed by the oxidation of a pair of cysteine residues. The resulting unit of
linked cysteines is called cystine. Extracellular proteins often have several disulfide bonds, whereas intracellular
proteins usually lack them.

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Peptide bond

The peptide bond is essentially planar. The oxygen has a partial negative charge and the nitrogen a partial positive
charge, setting up a small electric dipole.

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So due to the resonance peptide bonds are unable to rotate freely because of their partial double-bond character.
Rotation is permitted about the N-C and the C-C bonds. By convention, the bond angles resulting from
rotations at C-C are labeled (phi) and for the N-C bond (psi). Again by convention, both and are
defined as 1800when the polypeptide is in its fully extended conformation and all peptide groups are in the same
plane. In principle, and can have any value between -1800 and +1800, but many values are prohibited by steric
interference between atoms in the polypeptide backbone and amino acid side chains.

Ramachandran plot is used to determine secondary structure of protein and it is a graph between & .
The conformations of peptides are defined by the values of and . Conformations deemed possible are those that
involve little or no steric interference, based on calculations using known van der Waals radii and bond angles.

The areas shaded dark blue reflect conformations that involve no steric overlap and thus are fully allowed.
Medium blue indicates conformations allowed at the extreme limits for unfavorable atomic contacts.
The lightest blue area reflects conformations that are permissible if a little flexibility is allowed in the bond angles.

Two configurations are possible for a planar peptide bond. In the trans configuration, the two a-carbon atoms are on
opposite sides of the peptide bond. In the cis configuration, these groups are on the same side of the peptide bond.
Almost all peptide bonds in proteins are trans. This preference for trans over cis can be explained by the fact that

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steric clashes between groups attached to the a-carbon atoms hinder formation of the cis form but do not occur in the
trans configuration. By far the most common cis peptide bonds are X-Pro linkages.

Secondary structure of proteins includes the folding of the polypeptide chain only due to the

intramolecular H-bonding in peptide backbone i.e. between the carbonyl oxygen and NH grp.

- helix is a rod or twisted ribbons like structure which is a tightly coiled backbone forms the inner part of the
rod and the side chains extend outward in a helical array. The helix is stabilized by hydrogen bonds between the
NH and CO groups of the main chain. In particular, the CO group of each amino acid forms a hydrogen bond
with the NH group of the amino acid that is situated four residues ahead in the sequence.

Proline, rotation about the N-C bond is not possible. Thus, a Pro residue introduces a destabilizing kink in an
helix. In addition, the nitrogen atom of a Pro residue in peptide linkage has no substituent hydrogen to participate in
hydrogen bonds with other residues. For these reasons, proline is only rarely found within an helix or found in last.

Glycine occurs infrequently in helices for a different reason: it has more conformational flexibility than the other
amino acid residues. Polymers of glycine tend to take up coiled structures quite different from an - helix.

-conformation, the backbone of the polypeptide chain is extended into a zigzag rather than helical structure.
The zigzag polypeptide chains can be arranged side by side to form a structure resembling a series of pleats. In this
arrangement, called a sheet, hydrogen bonds are formed between adjacent segments of polypeptide chain.
The individual segments that form a - sheet are usually nearby on the polypeptide chain, but can also be quite
distant from each other in the linear sequence of the polypeptide; they may even be segments in different
polypeptide chains. The R groups of adjacent amino acids protrude from the zigzag structure in opposite directions,
creating the alternating pattern. The adjacent polypeptide chains in a sheet can be either parallel or antiparallel
(having the same or opposite amino-to-carboxyl orientations, respectively)

Tertiary structure of proteins defines the overall folding of polypeptide chain which is stabilized by
electrostatic interactions between opposite charged ionic grps, Vander walls forces, hydrophobic interaction,
hydrogen bonding. The 3-D folding of polypeptide chains is such that the interior contains predominantly
hydrophobic or nonpolar amino acids like leucine, phenylalanine while the polar, ionized hydrophilic residue
are found outside of the molecule so that they can compatible with aqueous environment.

Quaternary structure of proteins Some proteins consist of a single polypeptide chain, but others, called
multisubunit proteins, have two or more polypeptides associated noncovalently. Quaternary structure is only
restricted to the oligomeric proteins i.e. having more than one subunit or association of two or more
polypeptides held together by disulphide linkage, electrostatic interactions or H-bonding. The individual subunit in

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a multisubunit protein can be same or can be different e.g. Hemoglobin has four polypeptide chain i.e. 2 alpha ()
and 2 beta () while lactate dehydrogenase have four identical chains.

Methods of protein sequencing

1. From genetic code i.e. each triplet codes for a single amino acid, if we know the gene sequence then we
can predict the sequence of amino acids.
2. Fast atom bombardment mass spectroscopy & MALDI
3. Chemical methods
Edmanns method Phenylisothiocynate (most widely used)
Sangers method 1-fluro-2,4dinitrobenzene
Dansyl chloride Dimethylaminonapthanyl sulfonylchloride

These chemical methods sequence the amino acids from N-terminal sequence.

Sangers Dansyl chloride Edmanns reagent

The enzyme carboxypeptidases which are Exonuclease which sequentially removes carboxyl-terminal amino
acid residues from its peptide substrates, and require free - carbonyl grp. of the peptide chain. If the enzyme is
not able to do that means the carboxyl grp. is modified because it only need free carbonyl grp. or the terminal amino
acid is proline.

When the protein is larger than the protein is required to break into the small peptides and the each peptide
is sequenced by Edmanns reagent.

Trypsin - catalyze the hydrolysis of peptide bond on basic amino acids e.g. lysine and Arginine

CNBr Methionine

Chymotrypsin aromatic amino acids i.e. tyrosine, phenylalanine, tryptophan (heteroaromatic)

Agents such as urea or guanidinium chloride effectively disrupt the noncovalent bonds. They will
cause denaturation of protein.

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 The disulfide bonds can be cleaved reversibly by reducing them with a reagent such as b-mercaptoethanol.
In the presence of a large excess of b-mercaptoethanol, a protein is produced in which the disulfides
(cystines i.e. S-S grp) are fully converted into sulfhydryls (cysteines i.e. SH grp).

Some test for amino acids

1. Biuret test (copper sulphate) - compounds having two or more peptides give purple color
2. Millions reagent test (mercuric & mercurous nitrates in HNO3) - only for the amino acid which have
phenolic ring i.e. tyrosine (white ppt which on heating converted into red)
3. Xanthoprotic test (conc. HNO3) - for aromatic ring containing amino acids i.e. tyrosine, phenylalanine,
tryptophan which gives yellow color.

When the sequencing of the whole protein is done than protein structure is determined by NMR AND X-RAY
CRSTALLOGRAPHY.

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10 PHARMAGLIMPS- A GLIMPSE OF PHARMACY
In mammals, glucose is the only fuel that the brain uses under nonstarvation conditions and the only fuel that red
blood cells can use at all. Glycolysis is the sequence of reactions that metabolizes one molecule of glucose to two
molecules of pyruvate with the concomitant net production of two molecules of ATP. This process is anaerobic (i.e.,
it does not require O2) inasmuch as it evolved before the accumulation of substantial amounts of oxygen in the
atmosphere. Pyruvate can be further processed anaerobically (fermented) to lactate (lactic acid fermentation) or
ethanol (alcoholic fermentation). Under aerobic conditions, pyruvate can be completely oxidized to CO2, generating
much more ATP.

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Irreversible enzymes are (above performing reaction in Red):

1. Hexokinase
2. Phosphofructokinase (Rate limiting step)
3. Pyruvate kinase

Each NADH forms 3 ATP in ETC while FADH2 form 2ATP

The pentose phosphate pathway (HMP) is an alternative route for the metabolism of glucose. It does not
generate ATP but has two major functions: (1) The formation of NADPH for synthesis of fatty acids and
steroids and (2) the synthesis of ribose for nucleotide and nucleic acid formation. Genetic deficiency of glucose
6-phosphate dehydrogenase, the first enzyme of the pentose phosphate pathway, is a major cause of hemolysis of red
blood cells, resulting in hemolytic anemia.
In erythrocytes, the pentose phosphate pathway provides NADPH for the reduction of oxidized glutathione
catalyzed by glutathione reductase, a flavoprotein containing FAD. Reduced glutathione removes H2O2 in a
reaction catalyzed by glutathione peroxidase, an enzyme that contains the selenium analogue of cysteine
(selenocysteine) at the active site. This reaction is important, since accumulationof H2O2 may decrease the life span
of the erythrocyte by causing oxidative damage to the cell membrane, leading to hemolysis.

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 HMP pathway

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KERB CYCLE / TRI CARBOXYLIC ACID CYCLE / CITRIC ACID CYCLE

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 KERB / CITRIC ACID CYCLE

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 Enzymes
Enzymes are proteineous and highly specific biocatalyst which will lower the activation energy required for
conversion of substrate into the product by forming the complex with substrate molecule in the transition state
without affecting the equilibrium. Hence of binding enzyme and substrate always results in the releases the free
energy which will lower the activation energy.
A complete, catalytically active enzyme together with its bound coenzyme and/or metal ions is called a
holoenzyme. The protein part of such an enzyme is called the apoenzyme or apoprotein. A coenzyme (vitamins)
or metal ion (co-factor) that is very tightly or even covalently bound to the enzyme protein is called a prosthetic
group. Coenzymes act as transient carriers of specific functional groups on the substrate.

Classification of enzymes

Michalis Menton equation: Effect of substrate concentration on enzyme catalyzed

reaction

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MP SE ON PHARMACEU TICAL SCIENCES

Key points of Michalis-Menton equation

1. The enzyme catalysed reaction is mixed order i.e. first order at low substrate concentration because
active site has not be fully occupied by substrate molecules and zero order kinetics, when the substrate
concentration is very high then active site is fully occupied by the substrate molecule or the enzyme is
saturated.

2. The curve is hyperbola

Vmax represents the max. Velocity when all the active sites are occupied.
Vo represents the initial velocity
Km represents Michalis-Menton constant or affinity constant or the substrate concentration when initial velocity
is half of the maximum velocity. So unit of Km is [S]
Smaller the value of Km; higher will be affinity of enzyme towards substrate and hence rate of reaction
will be fast.
Higher the value of Km; smaller will be affinity of enzyme towards substrate and hence rate of reaction
will be slow.
Km varies from enzyme to enzyme; even isozymes may have different values of Km or different enzymes
may have same Km.
Turn over number (Kcat) is the maximum no. of moles of substrate that can be converted into product by
per mole of enzyme in unit time.

Kcat = Vmax / [Et]

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 Enzymes Can Be Inhibited by Specific Molecules

Enzyme inhibition can be either reversible or irreversible. An irreversible inhibitor dissociates very slowly from its
target enzyme because it has become tightly bound to the enzyme, either covalently or noncovalently. The
irreversible inhibitors are those that bind covalently with or destroy a functional group on an enzyme that is
essential for the enzymes activity, or those that form a particularly stable noncovalent association. Formation of a
covalent link between an irreversible inhibitor and an enzyme is common.
Some irreversible inhibitors are important drugs. Penicillin acts by covalently modifying the enzyme transpeptidase,
thereby preventing the synthesis of bacterial cell walls and thus killing the bacteria. Aspirin acts by covalently
modifying the enzyme cyclooxygenase, reducing the synthesis of inflammatory signals. Organophosphates bind
irreversible to acetylcholine esterase and results in organophosphate poisoning.
Reversible inhibition, in contrast with irreversible inhibition, is characterized by a rapid dissociation of the enzyme
inhibitor complex. The ffect of reversible inhibitor can be overcome either by dilution or dialysis of sample.
But irreversible not.

1. Competitive inhibition:
In competitive inhibition, an enzyme can bind substrate (forming an ES complex) or inhibitor (EI) but not both
(ESI). The competitive inhibitor resembles the substrate and binds to the active site of the enzyme. The substrate is
thereby prevented from binding to the same active site. A competitive inhibitor diminishes the rate of catalysis by
reducing the proportion of enzyme molecules bound to a substrate. At any given inhibitor concentration, competitive
inhibition can be relieved by increasing the substrate concentration. Under these conditions, the
substrate"outcompetes" the inhibitor for the active site. Km is increased and Vmax is constant. Methotrexate is
a structural analog of tetrahydrofolate, a coenzyme for the enzyme dihydrofolate reductase, which plays a role in

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the biosynthesis of purines and pyrimidines. It binds to dihydrofolate reductase 1000-fold more tightly than the
natural substrate and inhibits nucleotide base synthesis. It is used to treat cancer. Other example is ethanol and
methanol is
competitive inhibitor of alcoholdehydrogenase.

2. Noncompetitive inhibition

Noncompetitive inhibition, which also is reversible, the inhibitor and substrate can bind simultaneously to an
enzyme molecule at different binding sites because they dont have any structural similarity. A noncompetitive
inhibitor acts by decreasing the turnover number rather than by diminishing the proportion of enzyme molecules that
are bound to substrate. Here Km is constant and Vmax is decreased. Noncompetitive inhibition, in contrast
with competitive inhibition, cannot be overcome by increasing the substrate concentration. A more complex
pattern, called mixed inhibition, is produced when a single inhibitor both hinders the binding of substrate and
decreases the
turnover number of the enzyme.
[E] + [S] [ES] E+P

[I] [I]

[EI] [ESI]

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 3. Uncompetitive inhibition

Inhibitor will only bind to [ES] and lower both Vmax & Km

[E] + [S] [ES] E+P

[I]

[ESI]

Allosteric enzymes do not obey Michaelis-Menten kinetics. These enzymes consist of multiple subunits
and multiple active sites. Allosteric enzymes often display sigmoidal plots of the reaction velocity V 0 versus
substrate concentration [S], rather than the hyperbolic plots predicted by the Michaelis-Menten equation. In
allosteric enzymes, the binding of substrate to one active site can affect the properties of other active sites in the
same enzyme molecule. A possible outcome of this interaction between subunits is that the binding of substrate
becomes cooperative; that is, the binding of substrate to one active site of the enzyme facilitates substrate binding to
the other active sites.

Isoenzymes are multiple forms of an enzyme catalyzing same reaction. However, they differ in physical &
chemical properties which include structure, Km & Vmax values, pH optimum, relative susceptibility to inhibitors,
degree of denaturation and electrophoretic and immunological property.

h
When u your hundred percent
you put r n rest left is your luck
than c

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LIPIDS ARE CLASSIFIED AS SIMPLE OR COMPLEX

1. Simple lipids: Esters of fatty acids with various alcohols.

a. Fats: Esters of fatty acids with glycerol. Oils are fats in the liquid state.
b. Waxes: Esters of fatty acids with higher molecular weight monohydric alcohols.
2. Complex lipids: Esters of fatty acids containing groups in addition to an alcohol and a fatty acid.
a. Phospholipids: Lipids containing, in addition to fatty acids and an alcohol, a phosphoric acid residue. They
frequently have nitrogencontaining bases and other substituents, eg, in glycerophospholipids the alcohol is
glycerol and in sphingophospholipids the alcohol is sphingosine.
b. Glycolipids (glycosphingolipids): Lipids containing a fatty acid, sphingosine, and carbohydrate.
c. Other complex lipids: Lipids such as sulfolipids and aminolipids. Lipoproteins may also be placed in this
category.
3. Precursor and derived lipids: These include fatty acids, glycerol, steroids, other alcohols, fatty aldehydes,
and ketone bodies , hydrocarbons, lipid-soluble vitamins, and hormones. Because they are uncharged, acylglycerols
(glycerides), cholesterol, and cholesteryl esters are termed neutral lipids.

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Learn the unsaturated fatty acid name and how many double bonds
are present

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Phosphatidic acid is the base molecule for glycerophospholipids

Ceramide: is base molecule for spingolipids

Gangliosides have sialic acid (N-acetylneuraminic acid)

Globosides are neutral glycolipids as they have no charge at pH 7.

Phosphatidyl choline and ethanolamine are the glycerophospholipids which are neutral charge.

Lecithin are phosphatidyl choline which act as natural surfactant in lungs.

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 *EVOLUTION*

Very important classification (Try to learn the phospholipids which

are neutral at pH 7)

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 *

1. Role of phosphatidyl inositol

2. Role of arachidonic acid

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Vitamin A and D are hormone precursors

Vitamin D3 production and metabolism. (a) Cholecalciferol (vitamin D3) is produced in the skin by UV
irradiation of 7-dehydrocholesterol, which breaks the bond shaded. In the liver, a hydroxyl group is added at C-
25; in the kidney, a second hydroxylation at C-1 produces the active hormone, 1, 25-dihydroxycholecalciferol.
This hormone regulates the metabolism of Calcium in kidney, intestine, and bone. (b) Dietary vitamin D prevents
rickets, a disease once common in cold climates where heavy clothing blocks the UV component of sunlight
necessary for the production of vitamin D3 in skin.

Vitamin A1 and its precursor and derivatives. (a) -Carotene is the precursor of vitamin A1. Cleavage of -
carotene yields two molecules of vitamin A1 (retinol) (b). Oxidation at C-15 converts retinol to the aldehyde,

28 PHARMAGLIMPS- A GLIMPSE OF PHARMACY

 *
retinal (c), and further oxidation produces retinoic acid (d), a hormone that regulates gene expression. Retinal
combines with the protein opsin to form rhodopsin, a visual pigment widespread in nature. In the dark, retinal of
rhodopsin is in the 11-cis form (c). When a rhodopsin molecule is excited by visible light, the 11-cis-retinal
undergoes a series of photochemical reactions that convert it to all-trans-retinal (e), forcing a change in the
shape of the entire rhodopsin molecule.

Beta-oxidation
In -oxidationfatty acids undergo oxidative removal of successive two-carbon units in the form of acetyl-
CoA, starting from the carboxyl end of the fatty acyl chain. For example, the 16-carbon palmitic acid (palmitate at
pH 7) undergoes seven passes through the oxidative sequence, in each pass losing two carbons as acetyl-CoA. At the
end of seven cycles the last two carbons of palmitate (originally C-15 and C-16) remain as acetyl-CoA.

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30 PHARMAGLIMPS- A GLIMPSE OF PHARMACY
 Urea cycle

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Metabolism of phenylalanine

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Table1. Enzymes in diagnosis of diseases

1. -glutamyl transpeptidase Alcoholism

2. Aldolase Muscular dystrophy

3. SGOT Heart attacks (myocardial infarction)

4. SGPT Liver diseases (Hepatitis)

5. Creatinine phosphokinase Myocardial infarction (early marker)

6. Acid phosphates Cancer of Prostate gland

7. Lactate dehydrogenase Heart attacks, liver diseases

8. Alkaline phosphatase Rickets, obstructive jaundice

9. 5 nucleotidase Liver diseases

Table 2. Enzymes & genetic diseases

1. Tay-sachs N-acetyl hexoaminidase

2. Alkeptonuria Homogentisate dideoxygenase

3. Albinism Tyrosine -3-monoxygenase

4. Hartnups diseases Metabolism of tyrosine

5. Niemanns pick diseases Spingomylase

6. Lesh Nyhan syndrome Hypoxanthine-guanine phosphoribosyl

7. Van-giekes diseases Glucose-6-phosphatase (glycogen break down)

8. Phenylketouria Phenylalanine monoxygenase

9. Huler,s syndrome L-Iduronidase

10. Gaucher,s syndrome Gluco-cerebrosidase

11. Maple syrup urine diseases No decarboxylation of branched by alpha keto acid

dehydrogen

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Ta

ble 3. Vitamins

Vitamins Name/ Role Ring Deficiency diseases

1. Vitamin E Tocopherols Coumarin Antioxidant & Antifertility

2. Vitamin A Retinoids -ionone

3. Vitamin C Ascorbic acid Furazolidine Scurvy

4. Vitamin D Ergocalciferol (D2) & cholcaliferol (D3) Steroid nucleus Rickets & osteomalaceia

5. Vitamin B1 Thiamine (Aldehydes grp transfer) Thiazole Beri-Beri

6. Vitamin B2 Riboflavin (oxidation & reduction) Isoalloxazine Retina impairment

7. Vitamin B3 Nicotinic acid (oxidation & reduction) Pyridine Pellegra

8. Vitamin B4 Choline

9. Vitamin B5 Pantothenic acid (Acyl grp transfer) -mercapto ethylamine

10. Vitamin B6 Pyridoxal phosphate (Amino grp transfer) Anemia & peripheral neuropathy

11. vitamin B7 Biotin /vitamin H (Carboxyl grp transfer) Imidazole Dermatitis

12. Vitamin B9 Folic acid (one carbon grp transfer) Pteridine Megaloblastic anemia

13. vitamin B12 Cyano-cobalamine (1,2 H shift) Pernicious anemia

14. vitamin K Phylloquinone (K1) & Menaquinone (K2) -carboxylation of clotting factors

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 1. Imidazole grp - Histidine
2. Indole - Tryptophan
3. Phenolic grp - Tyrosine
4. Guanidino grp Arginine
5. Amide grp - Asparagine & Glutamine
6. Hydroxyl grp - Serine &Threonine
7. Thio grp /sulfhydryl- Cysteine
8. Thio ether - Methionine

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T

Table 5. Serological tests

1. Ducrey test Hemophilia

2. Vanden berg test Hepatitis
3. Widals test Typhoid
4. VDRL test Syphilis
5. Wassermann complement fixation test Syphilis
6. Mantauxs test & Tuberculin test Tuberculosis
7. Westrns test AIDS (for diagnosis)
8. ELISA AIDS
9. Fuji AIDS
10. Freis test Lymphogranuloma venerum
11. Ouchterlony test Smallpox
12. Schicks test Scarlet fever
13. Schultz charlatan test Scarlet fever
14. Radial immunodiffusion Influenza virus
15. Radial immune assay To detect HCG in serum of pregnant women as test for pregnancy
16. Cold hameagglutation test Pneumonia
17. Dicks test Diphtheria
18. Coombs test Brucellosis
19. Rose water test Rheumatic arthritis
20. Lepromine test Leprosy

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 1. Ven-den Bergh test Serum bilirubin

2. O-toludine test Glucose

3. Gerhards test Acetoacetate in urine

4. Mureoxide test Uric acid

5. Jeffs test Creatinine

6. Rothras test Ketone bodies

7. Saliwonoffs test Ketone bodies

8. Carr-price test Vitamin A

9. Heller nitric acid ring test Proteins

10. Sulfosalicylic acid test Proteins

11. Heat coagulation test Proteins

12. Biuret test & urease test urea

13. Salkowski test Sterols

14. Libermanns Buchard test cholesterol

15. Mac-clean test & Hapkins test Lactic acid

16. CNBr Nicotinic acid

17. Hays test Bile salts

18. Benzidine test Bile pigments

19. Sakaguchi test Urobillin

20. Raybins test Test for sucrose

21. Molish test Primary test for carbohydrates

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