This is the University of Mysore MSc. Biochemistry entrance exam syllabus:

University of Mysore MSc. Biochemistry entrance exam syllabus

M.Sc. Biochemistry Entrance Examination for the year 2013-14

ELIGIBILITY CRITERIA
1.The candidate should have studied B.Sc. with Biochemistry/Chemistry as a major/ optional.
2. The candidate shall have obtained a minimum of 45% (40% in case of SC/ST and Category I
candidates) of marks in cognate/optional subjects put together from all the years of the
examination of the course.
3. In case a candidate has taken longer than prescribed duration to pass the qualifying course, a
deduction of 3% from the percentage of the aggregate of marks of cognate/optional subjects for
every additional year shall be applied and the candidate should have obtained the minimum
marks prescribed even after such deduction to become eligible for admission.
4. The candidate seeking admission to M.Sc. Biochemistry shall have to appear for Entrance
Examination.
5. The date of the Entrance Examination will be given in the prospectus, will be notified on the
Department Notice board and also in the university web site.
6. The Entrance Exam shall be of 1 hr duration with 50 multiple choice questions of 1 mark each.
for a maximum of 50 marks.
7. The syllabus for the Entrance exam will be uploaded in the University web site.
8. The results of the Entrance exam will be announced in the Department Notice board and also
in the web site.
9. There shall be no provision for revaluation with respect to Entrance exam.
10. Entrance exam fee has to be paid through Demand Draft.
11. Fees paid for the Entrance examination is not refundable.
12. Marks list will be prepared by taking 50% of B.Sc. cognate/optional subject and 50% marks
obtained from the Entrance exam.
13. The candidate list – selection list/waiting list will be announced on the Department Notice
board and also in the web site.
14. Separate intimation will not be sent to the candidates.
SYLLABUS FOR M.SC. BIOCHEMISTRY
ENTRANCE EXAMINATION FOR THE YEAR 2013-14
UNIT I
BIO-INORGANIC CHEMISTRY & BIO-PHYSICAL CHEMISTRY
BIO-INORGANIC CHEMISTRY
1. Coordination Compounds:
Tansition metals,properties (Colour, Oxidation states,Magnetic Properties).
Coordinate bond,double and complex salts – differences with examples. Postulates of Werner’s
theory. Type of ligands, uni,bi and polydenate with examples. Coordination number.
Porphyrin nucleus and classification. Important metallo porphyrins occurring in naturestructure
and their biological importance (Hb,cytochrome,chlorophyll,Vit-B12).Bile pigments
chemical nature and their role.
2. Radiochemistry:
Natural and artificial radioactivity. Characteristics of radioactive elements, units of
radioactivity, disintegration constant,half life,alpha,beta and gamma radiations.Detection of
radioactivity by GM counter. Application of radioisotopes – 3H,
14 C, 131I,60CO,32 P. Biological effect of radioactivity. Safety measurements in handling radio
isotopes.
3. Nitrogen:
Fixation of atmospheric nitrogen – symbiotic and non – symbiotic. Nitrogen cycle,
environmental pollution by nitrogen compounds.
4. Phosphors:
Importance of phosphorus compounds in biological system, phosphorus cycle.
5. Oxygen:
Formation of Ozone in atmosphere. Role of ozone in maintenance of life on earth. Effects
of environmental pollutantson ozone layer.
6. Sulphur and Selenium:
Importance of compounds of sulphur and selenium in biological system. Effect of sulphur
compounds on environmental pollution.
7. Biochemistry Toxicology:
Toxicity of Lead,Mercury,Cadmium and Arsenic.
BIO-PHYSICAL CHEMISTRY
1.Concentration Units:
Avagadro’s number, Mole, Mole fraction, Molarity, Equivalent weight, Normality,
Molality (Problems to be worked out)
2. Collegative properties:
Osmotic pressure and its measurement by Berkely-Hartley method. Laws of osmotic pressure,
Hypo, Hyper and iostomic solution. effect of osmotic pressure on living cells. Donnan
membrane equilibrium. Relative lowering of vapour pressure, Roult’s law. Elevation of boiling
point, depression of freezing point and their application in determination of molecular weight.
Abnormal molecular weight, Van’t Hoff’s factor. Degree of association and dissociation.
3. Adsorption:
Freundlich’s and Langmuirs adsorption isotherm. Application of adsorption.
4. Viscosity:
Definition, determination of viscosity of liquids and solutions by Ostwald’s
viscometer(solutions of gum and protein to be taken as examples).
5. Distribution Law:
Distribution law, partition coefficient applications of distribution law.
6. Acid, bases, and buffers:
Lewis concept of acids and bases. Ionic product of water. PH scale, buffers, Henderson-
Hasselbach equation, buffer capacity. Preparation of acid and basic buffer solution. Theory of
acid base indicators. Choice of indicators. pH titration curve and isoelectric PH aminoacids.
7. Electrochemistry:
Specific,equivalent and molar conductance . Reference electrodes(hydrogen electrode and
calomel electrode). quinhydrone electrode.glass electrode determination of equivalent
conductance of a strong electrolyte. conductrometric titration( strong acid against strong
base,weak acid(amino acid)against NaOH) determination of pKa values of weak acids by
potentiometric titration.Determination of pH of a buffer by potentiometric method using
quinhydrone electrode.
8. Photochemistry:
Law of photochemistry, Quantum efficiency, light absorption, Beer-Lamberts law,
spectrophotometer, colorimeter. Fluorescence, phosphorescence, chemiluminescencs,
bioluminescence(Elementary treatment). Applications of UV-chemiluminescence spectra.
Principle of IR spectra and its applications.
UNIT II
BIO-ORGANIC- I
1.Introduction to Organic chemistry:
Classification of organic compound, Unique characteristics. IUPAC nomenclature of organic
compounds(including bifunctional).
2. Investigation of organic compounds:
Detection and quantitative estimation of element – nitrogen (estimation by Kjeldhl’s methods),
sulphur,phosphorus and halogens (problems to be solved).
3. Reaction Mechanism:
Concept of inductive effects and resonance. Classification of organic reactions.(substitution
addition, elimination and rearrangement),with one example for each. Concepts of the following –
carbocations,free radicals, carbenes, nucleophiles and electrophiles.
4. Aliphatic Hydrocarbons:
Dienes – types with examples, 1’3 butadiene, preparation (any one method), stability,
mechanism of addition of HBr, Diels – Alder reaction. Mechanism of Markownikoff and anti
Markownikoff addition of HBr to propane. Conformational analysis of ethane.
5. Cycloalkanes:
Reactivities and relative stabilities. Bayer’s strain theory. Sactise- Mohr theory.Boat and chair
forms of cycloalkanes . Axial and equatorial bonds.
6. ARENES
Structure of Benzene-by Resonance and Molecular Orbital Theories. Aromaticity. Mechanism
of Nitration and Friedel craft reaction. Electronic interpretation of the orientating influence of
substituents in the electrophilic substitution of toulelne, chlorobenzene, nitrobenzene, and phenol
Polynuclear hydrocarbons - Resonance structure of Naphthalene, Anthracene, Phenanthrene
and Diphenyl. Reaction-oxidation and nitration of sulphonation of naphthalene and oxidation of
Anthracene.
7. ALKYL HALIDES and Organ metallic Compounds
SN1 and SN2 reaction mechanism with one example each. Concept of elimination reaction
example – n butyl chloride. Application of organometallic compounds-organo lead,organo
lithium, cisplatin.
8. ALCOHOL
Classification. Monohydric alcohols – distingueishing reaction of 1o, 2 o and 3 o alcohol.
Dihydric alcohol – Glycol, preparation (any 2 method) and uses.
Trihydric alcohol- Glycerol, synthesis from propane, properties (reaction with concentrated
H2SO4, HNO3, Oxalic and HI
Ethanols – Acidity of phenols, effects of substation on acidity
9. STEREOCHEMISTRY
Stereoisomerism, types, Fischer-projection formulae, asymmetric carbon atom, molecular
dissymmetry, chirality, optical isomerism example: Glyceraldehydes, Lactic acid and Tartaric
acid. Nomenclature of enantiomers.D and L system, R and S system, Racemisation and
resolution.
UNIT III
BIOORGANIC II
1. HYDROXY ACID AND DICARBOXYLIC ACID
Structure and properties of :
a) Hydroxyl acids: Lactic acid, citric acid and isocitric acid
b) Dicarboxylic acid: Maleic and fumeric acid
c) Keto acids: Pyruvic,α-ketoglutaric , oxalo-acetic acid
2. AMINES
Classification, properties, amino functional group- Basicity of amines, acylation. Reaction with
HNO2 and Schiff’s base formation. Distinguishing reactions of primary, secondary and tertiary
amines.
3. HETEROCYCLIC COMPOUNDS
Occurrence, structural formula and importance of Furan, Pyrrole, Thiophene, Pyridine, Pyran,
Thiazole, Pyrimidine, Purine, Indole, Imidazole, Quinoline and Isoquinoline.
4. TERPENES
Isoprene rule, classification, structure, occurance and importance of
a) Mono terpenes - Limonene, Menthol and Camphor
b) Sesqui terpenes - Santonin, Juvenile Hormone-I and Absciscin -II
c) Di terpenes - Phytol
d) Triterpenes - Lanosterol
e) Tetra terpenes - Lycopine
f) Poly terpenes - Dolichols
5. STERIODS
Basic ring system in steroid. Structure and biological importance of Cholesterol, Ergosterol, Bile
Acids (Mono, Di, and Tricholic acid) and Ecdysone.
6. ALKALOIDS
Definition, classification based on their biological functions with example. Structure and
physiological action of LSD, Morphin, Nicotine, Atropine and Aristolochic Acid.
7. VITAMINS
Classification, water soluble and fat soluble. Structural formula and coenzyme forms of Vitamin
B1, B2, B6 and Niacin. Vitamin C as a redox reagent, properties and chemical synthesis.
Structural formula of vitamin A,D,E and K.
UNIT IV
BIOMOLECULES
CARBOHYDRATES
Carbohydrates-Classification, Biological importance
Monosaccharides: Configuration, relationship of D-Aldoses. General properties of Aldoses and
Ketoses-oxidation, reduction, reducing property,formation of gycolipides, acylation,
methylation, condensation-phenyl hydrazine, addition-HCN. Iterconversion of Aldoses and
ketoses by chemical method. Ascending and descending the series by chemical methods.
Stereochemistry of Monosaccharides, (+) and(-),D and L, Epimers, Anomers and
Diasterioisomers.
Glucose: Elucidation of open chain structure and ring structure of glucose. Conformation of
glucose(only structure).Mutarotation. Structure of Galactose, mannose, ribose and fructose.
Structure and biological importance of amino sugars, deoxy sugars, deoxy sugars, sugar
acids,neuraminic and muramic acid.
Disaccharides: Establishment of structure of sucrose and lactose. Biological importance and
structure of isomaltose, trehalose and maltose.
Polysaccharides: Partial structure, occurrence and importance of starch, glycogen, insulin,
cellulose, chitin and pectin.
Glycosaminoglycans: Occurrence, importance and structure of the repeating units of heparin,
hyaluronic acid, teichoic acid and choritin sulphate. Bacterial cell wall polysaccharides,
peptidoglycans.
Qualitative tests: Molish, Benedict’s, Fehling’s, picric acid, Barfoed’s, Bial’s, Selivanoff’s,
osazone tests.
AMINO ACIDS:
Structure and classification of amino acids based on polarity. Reactions of the amino groups
with HNO2, LiALH4. Ninhydrin, phenyl isothio cyanate, DANSYL chloride, flurodinitro
benzene, Zwitterionic properties, pKa values. Reaction of carboxy group hydrazine. Any
method for the chemical synthesis of amino acids. D and L notation.
Peptides:
Peptide bond, structure and biological importance of Glutothione, Valinomycin, Leuenkaphelin,
synthetic peptides-poly glutamic acid, polylysine. Chemical synthesis of dipeptides.
Proteins:
Isolation, methods of purification-dialysis salting out, pH precipitation and solvent
precipitation.
Classification of proteins based on solubility, structure and function with examples,
colour reactions of proteins-Biuret, Xanthoproteic, Million’s.
Primary structure of proteins, methods of determining N- and C- terminal amino acids,
amino acid composition, sequencing by Edman’s degradation method.
Secondary structure- α-Helix, β-sheet, β-bend. Tertiary and quaternary structure. 3 D
structure of Hemoglobin, Denaturation and renaturation of proteins. Anfinsen’s experiment.
UNIT V
LIPIDS, NUCLEIC ACIDS & BIOCHEMICAL TECHNIQUES
LIPIDS
Classification and biological role, Fatty acids- Nomenclature of saturated and unsaturated fatty
acids. Physical and chemical reactions, esterification, rancidity, essential fatty acids.
Aclglycerols: Saponification, saponification value, iodine value, acid value and significance.
Phosphoglycerides: Structure of lecithin, cephalins, phosphotidyl inositol, plasmalogens and
cardiolipin, biological role of phosphoglycerides.
Sphingolipids: Structure and importance of sphingomyelin.
Glycosphingo lipids: Structure and importance of gangliosides and cerebrosides.
Prostaglandins: Structure of PGE2 and PGF2, Biological roles of Thromboxane, Leukotrienes
and Prostaglandins.
Plasma lipoproteins: Types and functions.
Biological membrane: Composition of membrane, Fluid mosaic model, functions of the plasma
membrane – endocytosis, phagocytosis, membrane receptors and their functions.
NUCLEIC ACIDS:
(a) Isolation of DNA and RNA. Composition of DNA. Nucleosides and Nucleotides.
Chargaff’s rule. Watson and Crick model of DNA. Melting of DNA ™.
(b) RNA: composition, types (mRNA, tRNA and rRNA). Secondary structure of tRNA – clover
leaf model. Chemical reactions of RNA and DNA with acid and alkali. Color reactions of RNA
and DNA.
BIOCHEMICAL TECHNIQUES
General principles and procedures of chromatography – adsorption and partition. Techniques:
Paper chromatography – Ascending, descending and circular. 2D chromatography, Rf values,
column chromatography, principles and procedures of gel filtration, ion exchange
chromatography, affinity chromatography. TLC and their applications. Principles and procedures
of electrophoresis, paper and gel electrophoresis.
Centrifugation – Principle of differential centrifugation. Ultra centrifuge – construction and
applications.
UNIT VI
ENZYMOLOGY
1. Enzymes:
General characteristics, co-factors, co-enzymes and metal ions. Classification of enzymes based
on IUB with examples. Unit of enzyme activity – specific activity, enzyme specificity. Concept
of active site.
Theories of enzyme catalysis – Lock and key model, Koshland’s induced fit theory.
Enzyme kinetics – Factors affecting rate of enzyme catalyzed reactions.
Effect of substrate concentration, pH, temperature.
Michaelis-Menten equation (Derivation not required). Lineweaver-Burk (L-B) plot.
Determination of Vmax and km from L-B plot and their significance.
Allosteric properties – Sigmoidal curve, positive and negative modulators with PFK as an
example.
Iso enzymes – detection, nature, importance. LDH as an example.
Multi enzyme complex – pyruvate dehydrogenase complex – composition, subunits, assembly,
enzymatic reactions functions.
RNA as an enzyme (Ribozymes)
UNIT VII
METABOLISM
1.Metabolism
Anabolism, catabolism, stages. Compartmentalization of metabolic pathways.
2. Bioenergetics:
Laws of thermodynamics, first and second law. Concept of enthalpy, entropy and free energy.
Standardized free energy. Endergonic and exergonic reaction. Coupled reactions. High energy
compounds – structure of ATP and its free energy change during hydrolysis, other high energy
compounds.
3. Biological oxidation:
Ultra structure of mitochondria, Electron Transport Chain, Electron transport complexes.
Complex I, II, III and IV. Uncouplers and inhibitors of respiration (Rotenone, Actinomycin D,
Cyanide and 2, 4 DNP)
Oxidative phosphorylation, P/O ratio. Formation of ATP- Outline of Mitchell’s hypothesis.
Substrate-level phosphorylation with examples.
4. Metabolism of Carbohydrates:
Glycogen metabolism- glycogenolysis, glycogen synthesis. Glycolysis, energetic of glycolysis.
Entry of other carbohydrates into glycolytic pathway. Fates of Pyruvate-Conversion of Pyruvate
to lactate, alcohol and acetyl Co-A.
Citric acid cycle and its energetic. Amphibolic integrating roles of TCA cycle. Anaplerosis.
Pentose phosphate pathway and its significance. Cori cycle. Gluconeogenesis.
5. Lipid metabolism:
Oxidation of fatty acid- α, β and ω types. Β-oxidation of even number saturated fatty acids.
Energetic of β-oxidation.
Biosynthesis of even number fatty acids, Ketonebodies formation. Outline of cholesterol
biosynthesis.
6. Metabolism of Amino Acid:
General reaction of amino acid degradation- Transamination, deamination and decarboxylation.
Ketogenic and glucogenic amino acids. Urea cycle and its significance.
UNIT VIII
MOLECULAR BIOLOGY, GENETIC ENGINEERING & IMMUNOLOGY
MOLECULAR BIOLOGY
1. Degradation of Nucleic Acid
Degradation of nucleic acid by DNase and RNase and phosphodiesterase. Schematic pathway
for degradation of purines and pyrimidines (salvage pathway).
Central dogma of molecular Biology and its modification.
DNA as a genetic material
2. Replication of DNA:
Semi conservative mechanism. Meselson and Stahl experiment. Mechanism of Replication of
prokaryotic
3. Prokaryotic RNA Synthesis:
Role of RNA polymerase Initiation, elongation and termination. Reverse transcription.
4. Genetic code:
General features, Wobble hypothesis.
5. Prokaryotic Protein Biosynthesis:
Activation of Amino acids, Amino acyl tRNA synthesis. Initiation, elongation and termination
of protein synthesis.
6. Mutations:
Concept f mutation and mutagens- effect of HNO2, alkylating agents, intercalating agent and
UV-radiation. Concept of missense, nonsense, point mutation, frame shift mutation.
7. Concept of gene:
1) Gene expression in prokaryotes- concept of Lac operon.
2) Functional units in a typical eukaryotic gene-promotors, introns and exons.
GENETIC ENGINEERING
1. Historical development, aim and scope of genetic engineering
2. Isolation of DNA, cutting of DNA by restriction endonuclease- staggered cut and blunt end
3. Outline of Techniques of Genetic Engineering
Cutting genomic DNA, Separation of fragments by agarose gel electrophoresis.
Vector, plasmid: pBR 322, insertion of foreign DNA into Vectors.
Transfection of Vectors into host cells. cDNA principles of polymerase chain reaction and
application
4. Blotting Techniques
Principles and procedures of Southern and Northern blotting, Western blotting
5. Applications of Genetic Engineering
1) Transgenic plants, transgenic animals and gene therapy
2) Human genome project
IMMUNOLOGY
1. Immunity
Cellular and humoral immunity, cellular basis of immunity. Role of immunologically
important organs and cells bone marrow, thymus, spleen and lymphocytes. Formation
and function of T & B Lymphocytes and macrophages, Helper T-cells and killer T-cells.
2. Antigens
Definition, Haptenes, Epitopes, Antigens, Antigenicity.
3. Antibodies
Definition types and structure of a typical immunoglobulin (IgG-Light chain, heavy chain,
hyper-variable region, constant domains, Fab and Fc).
4. Anigen – Antibody reaction in Vitro
Formation of Antigen-Antibody complex. Application of immune diffusion, RIA, ELISA
(Basic principles only)
5. Immunization
Vaccination – vaccines and their preparations, Primary and secondary response.
6. Immunological disorders.
Allergy (hyper sensitivity reactions) – Types, AIDS-HIV Virus structure, mode of
transmission, mechanism-role of reverse trancriptase, clinical features, diagnosis, treatment.
UNIT IX
HUMAN PHYSIOLOGY AND CLINICAL BIOCHEMISTRY
HUMAN PHYSIOLOGY
1.Neurotransmission:
Type of neurons generalized structure of multipolar neuron. Resting membrane potential.
Action potential, transmission of a nerve impulse along an axon and across a synapse.
Neurotransmitters, Inhibitors of neuro transmitters.
2. Muscle:
Types of muscles and their structure. Ultrastructure of skeletal muscle. Contractile and
regulatory proteins of muscle, sliding filament model of skeletal muscle contraction.
3. Bone:
Composition and structure of long bone, growth and remodeling of long bone. Factors
affecting its growth.
4. Excretory system:
Structure of the Nephron, formation of urine-glomerular filteration, tubular reabsorption and
secretions.
5. Body Fluids:
Blood volume, composition and function. RBC, WBC and platelets, their structure functions.
Mechanism of blood coagulation. Biochemical events in transport of CO2 and O2 in blood.
Cerebrospinal fluid, lymph and its function. Blood brain barrier.
6. Acid base balance:
Maintenance of normal pH of the body fluids. Blood buffers. Role of lungs and kidney in
acid-base balance.
7. Endocrine system:
Endocrine organs, classification of hormones, Hierarchy, interplay and dynamic balance and
regulation of hormone secretions.
General mechanism of steroid hormone action. Mechanism of hormone action concept of
second messengers. Examples: cAMP, DAG, IP3, G-Protein.
8. Liver:
Structure of lobules functions – metabolic storage and detoxification.
CLINICAL BIOCHEMISTRY
1.Urine:
Normal composition of urine – volume, pH, colour, specific gravity. Constituents ; urea , uric
acid, creatinine, pigments, abnormal constituents – glucose, albumin, ketone bodies, variations in
urea, creatinine, pigments and their clinical significances in brief.
2. Blood:
Normal constituents of blood and their variation in pathological conditions – urea, uric acid
creatinine, glucose, bilirubin, Total protein, Albumin/Globulin ratio, Lipid profile – cholesterol,
triglycerides, lipoproteins HDL and LDL.
3. Liver function Tests:
Alkaline phosphatase, SGOT and SGPT
Cardiac injury profule CPK and LDH
4. Inborn errors of Metabolism
Sickle cell anemia, phenyl ketonuria, Nieman-pick disease.
UNIT X
NUTRITION AND MICROBIOLOGY
NUTRITION
1.Introduction
Concept of nutrition, calorific value of foods and its determination (Bomb calorimeter)
different components of energy expenditure respiratory quotient, Basal Metabolic Rate (BMR
determination of BMR, factors affecting BMR, specific dynamic action of food. Energy
expenditure at rest and work.
2.Carbohydrates
Dietary sources, dietary fibres and protein sparing action.
3. Proteins
Dietary sources, nutritional classification, nutritional value of proteins – PER, NPU and
Biological value of proteins (BV). Essential amino acids. Nitrogen balance mutual
supplementation of proteins, Malnutrition- Kwashiorkar and marasmus.
4. Fats
Dietary sources of fats, invisible fat, essential fattyacids and their biological importance.
5. Vitamins
Dietary sources, requirements, deficiency symptoms and biological role of water soluble
vitamins – Thiamine, Riboflavin, Niacin, Pantothenic acid, Pyridoxine, Biotin, Folic acid,
Vit.B12 and Vitamin C.
Fat soluble vitamins – Vitamin A,D,E and K.
Hypervitaminosis
6. Minerals
Mineral metabolism of Ca, P, Fe, Zn, Cu, I
7. Water metabolism:
Distribution of water in body fluids. Factors influencing water metabolism.
8. Antinutritional factors.
Sources and harmful effects of anti vitamins (Eg. Avidin, dicoumarol) Natural toxicants
(Eg.Lathyrus sativa) and adultrants (Eg. Butter yellow, lead chromate, malachite green)
9. Digestion absorption and transport of carbohydrates proteins and fats. GI tract, secretions,
composition and function of saliva, gastric, bile, pancreatic and intestinal juices. Appetite,
gastrointestinal hormones.
MICROBIOLOGY
1.Study of Microorganisms:
Staining microorganisms – Principle and procedure of gram stain, acid fast stain .
2. Microbial nutrition:
Growth of microorganisms, measurement of growth factors influencing growth-nutrition,
carbon source, nitrogen source. Temperature, pH and oxygen. Growth curve, phases of growth
curve.
3. Industrial Microbiology:
Production and importance – Alcoholic beverage (Beer and Wine), Fermented products of
milk, cheese, antibiotic production – penicillin, single cell protein – spirulina.
4. Antibiotics:
Definition, Mechanism of action of penicillin, streptomycin and chloramphenicol, antibiotic
resistance in brief.
5. Viruses
Classification based on genetic material with examples. Plant viruses – TMV. Morphology,
General characteristics and its replication.
6. Bacteriophages:
Morphology and general characteristics life cycle (Lysogeny and lytic cycle)of T even
bacteriophages.
PRACTICALS
Bio-inorganic Chemistry practical-1
1. Use of analytical balance and weighing.
2. Calibration, preparation of normal,Molar solution.
3. Preparation of standard sodium carbonate solution. Standardization of HO (Methyle
orange) and estimation of NaOH in the given solution (methyl orange or
phenolphthalein).
4. Calibration of volumetric glasswares.
5. Preparation of standard oxalic acid. Standardization of NaOH and estimation of H2SO4
in the given solution (phenolphthalein).
6. Preparation of standard oxalic acid. Standardization of KMnO4 and estimation of H2O2
in the given solution.
7. Preparation of standard K2Cr2O7. Standaradization of Na2S2O2 and estimation of CuSO4
in the given solution.
8. Preparation of standard K2Cr2O7. Estimation of ferrous (Fe2+)/ferric(Fe3+) ions in a
mixture using diphenylamine indicator.
9. Preparation of ZnSO4, standardization of EDTA and estimation of total hardness of water
using Erichorme black-T indicator.
10. Preparation of standard potassium biphthalate . standardization of NaOH and estimation
of HCl in the given solution(phenolphthalein).
PRACTICALS
Analysis of the following organic compounds;
Urea, Benzamide,Benzaldehyde, Aniline, Acetophenone, O-Cresol,
Nitrobenzene,Chlorobenzene, naphthalene, Toluidine, Benzoic icd, Salicylic acid, Resorcinol,
Benzyl alcohol, p-dichlorobenzene
PRACTICALS
ORGANIC PREPARATIONS
Preparation of
a) Benzoic acid from benzaldehyde or toluene
b) Meta dinitrobenzene from nitrobenzene
c) Aspirin from salicylic acid
d) Tribromophenol from phenol
e) P-Bromo acetanilide from acetanilide
f) Extraction of caffeine from tea leaves
g) Extraction of starch from potatoes
h) Extraction of casein from milk
i) Extraction of oil from oil seeds
Qualitative tests for ribose, deoxy ribose, mono, di and polysaccharides
PRACTICALS
PART-A (Biomolecules)
1.Qualitative analysis of Biomolecules
i) Carbohydrate – Glucose, Fructose, Lactose, Maltose and Sucrose.
ii) Amino acids and proteins – Arginine, Tryptophan, Tyrosine, Cystein, Albumin and
Casein.
iii) Nucleic acid – qualitative test for ribose and deoxy ribose.
iv) Lipids – Iodine value, saponification value, acid value.
2. Colorimetric estimation of
i) Glucose by DNA method
ii) Protein by Biuret method
iii) Protein by Lowry’s method
iv) Uric acid
v) Urea by DAMO method
vi) Creatinine by Jaffe’s method
vii) Phosphorus by Fiske and Subbarow’s method.
viii) Ferric iron by Thiocyanate method.
PART-B (Enzyme Assays)
1.Salivary Amylase
a) Determination of specific activity by DNS
b) Determination of pH optimum
c) Determination of Km and Vmax
d) Determination of initial velocity (time kinetics)
e) Determination of optimum temperature and energy of activation
PRACTICALS
Bio-chemistry of Nutrition and Human Physiology
1. Determination of
a.Moisture content of foods.
b.Adulterants in foods
c.Calcium in Ragi.
d.Iron in Drumsticks
2. Estimation of vitamin-C in lemon and gooseberries
3. Gravimetric estimation sulphate.
4. Qualitative analysis of urine-detection of urea,uric acid and creatinene
5 Qualitative analysis of abnormal constituents in urine-glycose,albumine,bile
pigments,bile salts and ketone bodies.
6. Determination of titrable acidity of urine.
7. Estimation of reducing sugars by Hegedon and Jensen method
8. Estimation of amino acid by formal titration
9. Determination of saponification value of oil or fat
10. Determination of iodine value of oil or fat.
PART – B
Bio-Physical – II Microbiology
1. Determination of equivalent – conductance of strong electrolyte by wheat stones bridge
(Kohlrainnsch’s bridge).
2. conductometric titration of strong acid against strong base.
3. Preparation of acidic and basic buffers and determination pH using pH meter
4. Determinatio of Pka value of amino acid by using pH meter or potentio meter.
5. Determination of ph of a buffer solution by potentio metric method using quinhydrone
electrode.
6. Gram staining.
7. Growing microbes from soil and sewage water.
8. Demonstration of western blotting.
9. Extraction and estimation of DNA from coconut ensosperm.
10. Extraction and estimation of RNA from spinach leaves.