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DEPARTMENT OF BIOCHEMISTRY

B.Sc First Year BIOCHEMISTRY SEMESTER I PAPER I SYLLABUS 20 Unit I : Carbohydrates and Lipids 30hours

Water as a biological solvent and its role in biological processes. Carbohydrates: Classification, monosaccharides, D and L designation, open chain and cyclic structures, epimers and anomers,mutarotation, reactions of carbohydrates (due to functional groups - hydroxyl , aldehyde and ketone). Amino sugars, Glycosides. Structure and biological importance of disaccharides (sucrose, lactose, maltose, isomaltose, trehalose), trisaccharides (raffinose, melezitose), structural polysaccharides (cellulose, chitin, pectin) and storage polysaccharides (starch, inulin, glycogen). Glycosaminoglycans, Bacterial cell wall polysaccharides. Outlines of glycoproteins, glycolipids and blood group substances. Lipids: Classification, saturated and unsaturated fatty acids, structure and properties of fats and oils (acid, saponificition and iodine values, rancidity). General properties and structures of phospholipids, sphingolipids and cholesterol. Prostaglandins- structure and biological role of PGD 2 ,PGE 2 and PGF 2 . Lipoproteins: Types and functions Biomembranes: Behavior of amphipathic lipids in water- formation of micelles, bilayers, vesicles, liposomes. Membrane composition and organization Fluid mosaic model.

Unit-II : Amino Acids, Peptides and Proteins pH, Buffers, Henderson- Hasselbalch equation.

30 hours

Amino Acids: Classification, structure, stereochemistry, chemical reactions of amino acids due to carbonyl and amino groups. Titration curve of glycine and pK values. Essential and non-essential amino acids, non-protein amino acids. Peptide bond - nature and conformation. Naturally occurring peptides glutathione, enkephalin. Proteins: Classification based on solubility, shape and function. Determination of amino acid composition of proteins. General properties of proteins, denaturation and renaturation of proteins. Structural organization of proteins- primary, secondary, tertiary and quaternary structures (Eg. Hemoglobin and Myoglobin), forces stabilizing the structure of protein. Outlines of protein sequencing. **********

DEPARTMENT OF BIOCHEMISTRY

B.Sc First Year BIOCHEMISTRY SEMESTER I I PAPER I SYLLABUS 2011-2012 Unit-III : Nucleic Acids and Porphyrins 25 hours Nature of nucleic acids. Structure of purines and pyrimidines, nucleosides, nucleotides. Stability and formation of phosphodiester linkages. Effect of acids, alkali and nucleases on DNA and RNA. Structure of Nucleic acids- Watson-Crick DNA double helix structure, introduction to circular DNA, super coiling, helix to random coil transition, denaturation of nucleic acids- hyperchromic effect, Tm-values and their significance. Reassociation kinetics, cot curves and their significance. Types of RNA and DNA . Prophyrins: Structure, properties and functions of heme, chlorophylls and cytochromes.

Unit-IV : Enzymes

35 hours

Introduction to biocatalysis, differences between chemical and biological catalysis. Nomenclature and classification of enzymes. Enzyme specificity. Active site. Principles of energy of activation, transition state. Interaction between enzyme and substrate- lock and key, induced fit models. Definition of holoenzyme, apo-enzyme , coenzyme, cofactor. Fundamentals of enzyme assay, enzyme units. Factors affecting the catalysis- substrate concentration, pH, temperature. Michaelis - Menten equation for uni-substrate reaction (derivation not necessary), significance of K M and V max . Enzyme inhibitionirreversible and reversible, types of reversible inhibitions- competitive and non-competitive. Outline of mechanism of enzyme action- acid-base catalysis, covalent catalysis, electrostatic catalysis, and metal ion catalysis. Regulation of enzyme activity- allosterism and cooperatitvity, ATCase as an allosteric enzyme, covalent modulation- covalent phosphorylation of phosphorylase, zymogen activationactivation of trypsinogen and chymotrypsinogen. Isoenzymes (LDH). Multienzyme complxes (PDH). Ribozyme . ************

DEPARTMENT OF BIOCHEMISTRY

2011-2012 1st Year Practicals Paper-I: Qualitative Analysis and Enzymology 90 hrs
(3 hrs/week)

Introduction to Good Laboratory Practice (GLP). Principles of Laboratory Hygiene and Safety. List of experiments: 1. Preparation of buffers (acidic, neutral and alkaline) and determination of pH. 2. Qualitative identification of carbohydrates- glucose, fructose, ribose/xylose, maltose, sucrose, lactose, starch/glycogen. 3. Qualitative identification of amino acids histidine, tyrosine, tryptophan, cysteine, arginine. 4. Qualitative identification of lipids- solubility, saponification, acrolein test, Salkowski test, Lieberman-Burchard test. 5. Preparation of Osazones and their identification. 6. Absorption maxima of colored substances- p-Nitrophenol, Methyl orange. 7. Absorption spectra of protein-BSA, nucleic acids- Calf thymus DNA. 8. Titration curve of glycine and determination of pK and pI values. 9. Assay of amylase 10. Assay of urease 11. Assay of catalase. 12. Assay of phosphatase 13. Determination of optimum temperature for amylase. 14. Determination of optimum pH for phosphatase. *****************

DEPARTMENT OF BIOCHEMISTRY

B.Sc II Year BIOCHEMISTRY SEMESTER III PAPER I I SYLLABUS 2011-2012

Unit- I : Bioenergetics and Biological Oxidations

30 hours

Energy transformations in the living system, Free energy concept. Exergonic and endergonic reactions. High energy compounds. Phosphate group transfer potential. Substrate level phosphorylation. Biological oxidations: Definition, enzymes involved- oxidases, dehydrogenases and oxygenases. Redox reactions. Redox couplers. Reduction potential (, o , biochemically important half reactions.

o ). Standard reduction potential ( o ) of some

Ultra structure of mitochondria. Electron transport chain and carriers involved. Oxidative phosphorylation, theories of oxidative phosphorylation- Mitchells chemiosmotic theory. F o F 1 - ATPase. Inhibitors of respiratory chain and oxidative phosphorylation, uncouplers. Formation of reactive oxygen species and their disposal through enzymatic reactions. Ultra structure of chloroplast, Cyclic and non-cyclic photophosphorylation.

Unit- II : Carbohydrate and Lipid Metabolism

30 hours

Concept of anabolism and catabolism. Glycolytic pathway, energy yield. Fate of pyruvate- formation of lactate and ethanol, Pasteur effect. Citric acid cycle, regulation, energy yield, amphipathic role. Anaplerotic reactions. Glycogenolysis and glycogenesis. Pentose phosphate pathway. Gluconeogenesis. Photosytnthesis- Light and Dark reactions, Calvin cycle, C 4 Pathway. Catabolism of fatty acids (- oxidation) with even and odd number of carbon atoms, Ketogenesis, de novo synthesis of fatty acids, elongation of fatty acids in mitochondria and microsomes, Biosynthesis and degradation of triacylglycerol and lecithin. Biosynthesis of cholesterol.

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DEPARTMENT OF BIOCHEMISTRY

B.Sc II Year BIOCHEMISTRY SEMESTER IV PAPER II SYLLABUS 2011-2012

Unit-III : Metabolism of Nitrogen Compounds

30 hours

General reactions of amino acid metabolism- transamination, decarboxylation and deamination, Urea cycle and regulation, Catabolism of carbon skeleton of amino acids- glycogenic and ketogenic amino acids. Metabolism of glycine, serine, aspartic acid, methionine, phenylalanine and leucine. Biosynthesis of creatine. Inborn errors of aromatic and branched chain amino acid metabolism. Biosynthesis and regulation of purine and pyrimidine nucleotides, de novo and salvage pathways. Catabolism of purines and pyrimidines. Biosynthesis of deoxyribonucleotides- ribonucleotide reductase and thymidylate synthase and their significance. Disorders of nucleotide metabolism- Gout, LeschNyhan syndrome. Biosynthesis and degradation of heme

Unit-IV : Biochemical Techniques

30 hours

Methods of tissue homogenization: (Potter-Elvejham, mechnical blender, sonicator and enzymatic). Principle and applications of centrifugation techniques- differential, density gradient. Ultracentrifugation- preparative and analytical.. Principle and applications of chromatographic techniques- paper, thin layer, gel filtration, ion- exchange and affinity chromatography. Elementary treatment of an enzyme purification. Electrophoresis- principles and applications of paper, polyacrylamide (native and SDS) and agarose gel electrophoresis. Colorimetry and Spectrophotometry- Laws of light absorption- Beer-Lambert law. UV and visible absorption spectra, molar extinction coefficient, biochemical applications of spectrophotometer. Principle of fluorimetry. Tracer techniques: Radio isotopes, units of radio activity, half life, and - emitters, use of radioactive isotopes in biology.

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DEPARTMENT OF BIOCHEMISTRY

2011-2012 2nd Year Practical Paper-II: Quantitative Analysis and Biochemical Techniques List of Experiments: 90 hrs
(3 hrs/week)

1.Estimation of amino acid by ninhydrin method. 1. Estimation of protein by Biuret method. 2. Estimation of protein by Lowry method. 3. Estimation of glucose by DNS method. 4. Estimation of glucose by Benedicts titrimetric method. 5. Estimation of total carbohydrates by anthrone method. 6. Isolation of egg albumin from egg white. 7. Isolation of cholesterol from egg yolk. 8. Isolation of starch from potatoes. 9. Isolation of casein from milk. 10. Separation of amino acids by paper chromatography. 11. Determination of exchange capacity of resin by titrimetry. 12. Separation of serum proteins by paper electrophoresis. 13. Separation of plant pigments by TLC.

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DEPARTMENT OF BIOCHEMISTRY

B.Sc III Year BIOCHEMISTRY SEMESTER V PAPER III SYLLABUS 2011-2012

Unit- I : Physiology

24 hours

Digestion and absorption of carbohydrates, lipids and proteins. Composition of blood and coagulation of blood. Hemoglobin and transport of gases in blood (oxygen and CO 2 ). Heart- structure of the heart, cardiac cycle, cardiac factors controlling blood pressure. Muscle- kinds of muscles, structure of myofibril, organization of contractile proteins and mechanism of muscle contraction. Endocrinology- organization of endocrine system. Classification of hormones. Outlines of chemistry, physiological role and disorders of hormones of pancreas, thyroid, parathyroid, gonads, placenta, adrenals, pituitary and hypothalamus. Introduction of gastrointestinal hormones. Mechanism of hormonal action- signal transduction pathways for adrenaline, glucocorticoids and insulin.

Unit- II : Nutrition

21 hours

Balanced diet. Calorific values of foods and their determination by bomb calorimeter. BMR and factors affecting it. Specific dynamic action of foods. Energy requirements and recommended dietary allowance (RDA) for children, adults, pregnant and lactating women. Sources of complete and incomplete proteins. Biological value of proteins. Role of essential fatty acids in human nutrition. Malnutrition- Kwashiorkar, Marasmus and PEM. Vitamins- sources, structure, biochemical roles, deficiency disorders of water and fat soluble vitamins. Introduction to neutraceutical and functional foods. Bulk and trace elements-Ca, Mg, Fe, I, Cu, Mo, Zn, Se and F. Obesity and starvation.

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DEPARTMENT OF BIOCHEMISTRY

B.Sc III Year BIOCHEMISTRY SEMESTER VI PAPER III SYLLABUS 2011-2012

Unit- III : Clinical Biochemistry

23 hours

Plasma proteins in health and disease. Disorders of blood coagulation (haemophilia). Types of anemias, haemoglobinopathies-sickle cell anemia and thalassemias. Structure and functions of the liver. Liver diseases-jaundice, hepatitis, cirrhosis. Liver function testsconjugated and total bilurubin in serum, albumin: globulin ratio, hippuric acid and bromsulphthalein tests. Serum enzymes in liver diseases- SGPT, GGT and alkaline phosphatase. Kidneys-structure of nephron, urine formation, normal and abnormal constituents of urine. Biological buffers. Role of kidneys in maintaining acid-base and electrolyte balance in the body. Renal function tests- creatinine and urea clearance tests, phenol red test. Disorders of carbohydrate metabolism- hypoglycemia, hyperglycemia, glycosuria, renal threshold value. Diabetes mellitus-classification, glucose tolerance test (GTT), diabetic ketoacidosis. Disorders of lipid metabolism- plasma lipoproteins, lipoproteinemias, fatty liver, hyper cholesterolemia, atherosclerosis. Biochemical tests for the diagnosis of heart diseases- HDL/LDL cholesterol, SGOT, LDH, CK, C-reactive protein, cardiac troponins. Unit- IV : Immunology 22 hours

Organization of immune system. Organs and cells of immune system. Innate and acquired immunity. Cell mediated and humoral immunity (T- and B- cells). Classification of immunoglobulins, structure of IgG. Epitopes / antigenic determinants. Concept of haptens. Adjuvants. Theories of antibody formationclonal selection theory. Monoclonal antibodies. Antigen-antibody reactions- agglutination, immunoprecipitation, immunodiffusion. Blood group antigens. Immunodiagnostics-RIA, ELISA. Vaccines and their classification. Traditional vaccines-live and attenuated, toxoids. Modern vaccines- recombinant and peptide vaccines. Outlines of hypersensitivity reactions. Fundamentals of graft rejection and MHC proteins. **************

DEPARTMENT OF BIOCHEMISTRY

2011-2012 3rd Year Practical -III: Nutritional and Clinical Biochemistry 90 hrs List of Experiments:
(3 hrs/week)

1. Estimation of calcium by titrimetry 2. Estimation of iron in apple juice by phenanthroline method. 3. Estimation of sodium by flame photometry. 4. Estimation of vitamin C by 2, 6 -dichlorophenol indophenol method. 5. Isolation of total lipids by gravimetric method. 6. Determination of iodine value of an oil. 7. Determination of acid value of an oil. 8. Estimation of hemoglobin in blood. 9. Total count - RBC and WBC. Differential count. 10. Determination of blood group and Rh typing. 11. Visualization of antigen antibody reactions (Ouchterlony technique). 12. Urine analysis for albumin, sugars and ketone bodies. 13. Estimation of urinary creatinine. 14. Estimation of blood urea. 15. Estimation of serum total cholesterol. 16. . Determination of serum alkaline phosphatase activity. 17. Determination of SGOT and SGPT activity

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DEPARTMENT OF BIOCHEMISTRY

B.Sc III Year BIOCHEMISTRY SEMESTER V PAPER IV SYLLABUS 2011-2012

Unit- I : Microbiology

24 hours

Introduction to brief history of microbiology. Classification of microorganisms- prokaryotic and eukaryotic microorganisms. Isolation and cultivation of bacteria. Selective media and enriched media. Bacterial growth curve and kinetics of growth. Batch, continuous and synchronous cultures. Grams staining- Gram positive and Gram negative bacteria, motility and sporulation. Industrial uses of Aspergillus niger, yeast and Spirulina. Structure and composition of viruses. One-step growth and determination of plaque forming units (PFU). Isolation and cultivation of bacterial plaques. Lytic and lysogenic life cycle of phage. TMV, Retro viruses- HIV. Prions and Mycoplasma.

Unit- II : DNA Replication and Transcription

21 hours

Organization of genome in prokaryotes and eukaryotes. Experimental evidences to prove nucleic acids as genetic material. Nature and structure of the gene. DNA replication- models of replication, MeselsonStahls experimental proof for semi-conservative model. DNA polymerases I, II and III of E.coli, helicase, topoisomerases, primase, ligase. Bidirectional replication model. Okazaki fragments, leading and lagging strands of DNA synthesis. Inhibitors of DNA replication. Transcription - RNA synthesis, RNA polymerases of prokaryotes. Promoters, Initiation- sigma factors and their recognition sites. Elongation- role of core enzyme. Termination- rho dependent and rho independent. RNA polymerase I, II and III of eukaryotes. Transcriptional events in eukaryotic m-RNA synthesis, post-transcriptional modifications of eukaryotic m-RNA. Inhibitors of RNA synthesis.

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DEPARTMENT OF BIOCHEMISTRY

B.Sc III Year BIOCHEMISTRY SEMESTER VI PAPER IV SYLLABUS 2011-2012

Unit- III : Protein Synthesis and Regulation of Gene Expression

21 hours

Introduction to protein synthesis- Genetic code, structure of t-RNA, deciphering of genetic code, Nirenbergs and Khoranas experiments, wobble hypothesis, degeneracy of genetic code. Protein synthesis- activation of amino acids (aminoacyl t-RNA synthetases). Ribosome structure. Initiation, elongation and termination of protein synthesis. Post- translational modifications- signal hypothesis. Inhibitors of protein synthesis. Regulation of prokaryotic gene expression- induction and repression. Lac operon, catabolite repression. Tryptophan operon and attenuation.

Unit- IV : Recombinant DNA technology

24 hours

Outlines of cloning strategies. DNA sequencing- Maxam Gilbert and Sangers methods. Tools of r-DNA technology: Enzymes- Restriction endonucleases, ligase, phosphatases, reverse transcriptase, polynucleotide kinases, terminal transferase nucleases-S 1 and RNAase H. Restriction mapping. Cloning vectors- Plasmids, Ti plasmids, Cosmids, phages, shuttle vectors, expression vectors. Host- E.coli, Sacchromyces cereviciae, Agrobacterium tumifaciens. Construction of c-DNA and genomic libraries. Isolation and sequencing of cloned genes- colony hybridization, nucleic acid hybridization, hybrid released translation (HRT) and hybrid arrested and released translation (HART) using reporter genes [- galactosidases, green fluorescent proteins (GFP)]. Polymerase chain reaction- principle and applications. Outlines of blotting techniques-Southern, Northern and Western. Applications of gene cloning- production of insulin and human growth hormone, production of Bt cotton and edible vaccines.Introduction to Bioinformatics- definitions of proteomics and genomics. Gene bank, NCBI, DDBJ, Swissprot, PDB. Sequence alignments- BLAST and FASTA.

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DEPARTMENT OF BIOCHEMISTRY

2011-2012 3rd Year Practical Paper-IV: Microbiology and Molecular Biology 90 hrs
(3 hrs/week)

List of Experiments:

1. Preparation of culture media and sterilization methods. 2. Isolation of pure cultures: (i) Streak plate method. (ii) Serial dilution method. 3. Gram staining. 4. Motility of bacteria by hanging drop method. 5. Bacterial growth curve. 6. Antibiotic sensitivity by paper disc method. 7. Isolation of DNA from onion/liver/coconut endosperm. 8. Isolation of plasmids. 9. Determination of purity of nucleic acids by UV-spectrophotometric method. 10. Estimation of DNA by diphenylamine method. 11. Estimation of RNA by orcinol method. 12. Electrophoresis of nucleic acids and visualization by methylene blue staining. 13. Restriction mapping: - DNA with any two restriction enzymes. 14. Sequence alignments of insulin/BSA with other proteins using BLAST and FASTA.

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I B.Sc; BIOCHEMISTRY-PAPER-I
I SEMESTER MODEL QUESTION PAPER 2011-12 (Carbohydrates,Lipids,Aminoacids,Peptides)

Time:3hrs PART-1

Maximum marks:75

Answer any THREE questions choosing at least one question from each section 10X3=30 Marks
SECTION A(CARBOHYDRATES AND LIPIDS) 1.Describe the bacterial cell wall polysaccharides. 2.write an account on structure of prostaglandins and biological role of PGD 2 ,PGE 2 . 3.Describe the molecular structure of fluid mosaic model of plasma membrane SECTION-B(Amino Acids,Peptides and Proteins) 4.Classify the Amino Acids basing on t heir structure. 5.Describe the quarte ary structure of proteins. 6.Describe various chemical reactions of amino acids.

PART-2
Answer any FIVE questions.(Short answer questions) 7.Structure and biological importance of disaccharides. 8.Mutarotation. 9.Lipoproteins-Types and functions. 10.Henderson-Hasselbalch equation 11.Peptide-Glutathione. 12.Classification of proteins based on function. 13.Protein Sequencing. 14.General Properties and structure of Sphingolipids. 5x5=25 Marks

PART-3
Answer any TEN questions.(Very short answer questions) 10x2=20 Marks 15.Anomers. 16.Structure of Sedoheptulose,Lyxose. 17.Glycoprotein s. 18.Saponification. 19.Structure of Cholestrol. 20.Essential and non-essential amino acids. 21.Factors stabilizing structure of protein. 22.Aromatic amino acids. 23.Water as biological solvent. 24.Classification of proteins basing on shape. 25.Peptide bond. 26.Micelle. Note:5 marks and 2 marks questions should be given from Unit I and Unit II with equal weihtage. *****

I B.Sc; BIOCHEMISTRY-PAPER-I
II SEMESTER MODEL QUESTION PAPER 2011-12 (NUCLEIC ACIDS AND PORPHYRINS,ENZYMES)

Time:3hrs PART-I

Maximum marks:75

Answer any THREE questions choosing at least one question from each section 10x3=30 Marks SECTION-A
1.Write an account on Watson Crick DNA double helix structure. 2.Explain the structure,properties and functions of Heme. 3.Derive Michaclis-Menten equation for uni-substrate reaction.

SECTION-B
4.What are multienzyme complexes? Explain PDH. 5. Explain lock and Key mechanism of enzyme substrate reactions. 6.Write an essay on enzyme inhibition.

PART-II
Answer any five questions 7.Enzyme specificity and active site. 8.Types of RNAs and their functions. 9.Properties of Cytochromes. 10.Factors effecting the catalysis. 11.Competitive inhibition of enzymes. 12.Electrostatic catalysis of enzymes. 13.Super coiling of DNA. 14.Classification of enzymes. 5x5=25Marks

PART-III
Answer any TEN questions
15.Ribozyme. 16.Stability and formation of phosohodiester bond. 17.Structure of chlorophyll. 18.Tm-Value of DNA. 19.Structures of purines. 20.Holoenzyme. 21.Types of reversible inhibitions. 22.Allosterism. 23.Significance of K m and V max. 24.Activation of trypsinogen and chymotrypjnogen. 25.Cofactor. 26.Hyperchromic effect. Note:5 Marks and 2 Marks questions should be given from Unit I and Unit II with equal weightage.

10x2=20Marks

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II B.Sc; BIOCHEMISTRY-PAPER-II
Time:3hrs III SEMESTER MODEL QUESTION PAPER-2011-12 (BIOENERGETICS AND METABOLISM) Maximum marks:75 MARKS

PART-I
Answer any THREE questions choosing atleast one question from each section 10x3=30Marks SECTION-A(Bioenergitics)
1.Explain the role of enzymes involved in oxidative phosphorylation. 2.Describe the ultra structure of chloroplast. 3.Write an account on mitochondrial electron transport.

SECTION-B(Carbohydrates and lipid metabolism)


4.Describe the citric acid cycle and its regulation. 5.Give a detailed account on biosynthesis of cholesterol. 6.What is .Oxidation ?Explain the Oxidation process of fatty acids with even number of carbon atoms.

PART-II(Short answer questions)


Answer any FIVE questions.
7.High energy compounds. 8.Mitchells chemiosmotic theory. 9.C 4 .Path way. 10.Cytochromes. 11.Photophosphorylation. 12.Gluconeogenesis. 13.Synthesis of triglyserides. 14.Glycolytic pathway.

5x5=25 Marks

PART-III(Very short answer questions)


Answer any TEN questions
15.Substrate level phosphorylation. 16.Exogenic and Endogenic reactions. 17.Biological Oxidation . 18.Dehydrogenases. 19.Uncouplers. Ketogenesis. 22.Anaplerotic reactions. 23.Lecithin. 24.RUBP. 25.Glycogenolysis. 26.Microsomes.

10x2=20 Marks

NOTE:5 and 2 Marks Questions should be given from Unit Iand Unit II with equal weightage.

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II B.Sc; BIOCHEMISTRY-PAPER-II
Time:3hrs IVSEMESTER MODEL QUESTION PAPER-2011-12 (METABOLISM AND BIOCHEMICAL TECHNIQUES) Maximum marks:75 MARKS

PART-I
Answer any THREE questions choosing atleast on question from each section 10x3=30 Marks

SECTION-A(Metabolism of nitrogen compounds)


1.Mention the inborn errors of aromatic and Branched chain amino acid metabolism. 2.Describe the biosynthesis and Degradation of Heme. 3.Explain the biosynthesis of purines by denovo pathway.

SECTION-B(Biochemical Techniques)
4.What is electrophoresis?Explain in detail Agarose Gel Electrophoresis. 5.Explain the principle and applications of Ion exchange chromatography. 6.What is spectrophotometer ?Give an account of Biochemical applications of Spectrophotometer. PART-II(Short answer questions)

Answer any FIVE questions.


7.Urea cycle. 8.Biosynthesis of creatine. 9.Lesch-Nyhan syndrome . 10.Decarboxilation reaction of amino acid metabolism. 11.Tissue homogenation methods. 12.Thin layer chromatography and Its applications. 13.Beer-Lamberts law. 14.Principle of fluorimetry.

5x5=25 Marks

PART-III(Very short answer questions)


Answer any TEN questions. 10x2=20 Marks
15.Molar extinction coefficient. 16.Glucogenic and Ketogenic amino acids. 17.Thymidilate synthase. 18.Density gradient centrifugation. 19.Radio isotopes. 20.PAGE. 21.Regulation of pyrimidine synthesis. 22.Deamination reactions of amino acids. 23.Serine. 24.Mechanical blender. 25.Applications of electrophoresis. 26.Gout. Note:5and 2 Mark Questions should be given from Unit-I and Unit-II with equal weightage.

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III B.Sc; BIOCHEMISTRY-PAPER-III V SEMESTER MODELQUESTION PAPER 2011-12 (Physiology and Nutrition)

Time:3hrs Section-A Answer all questions

Maximum marks:75 4x10=40 Marks

1.Explain the process involved in coagulation of blood. (or) Describe the process of digestion and absorption proteins. 2.Describe the structure of myofibril and discuss the mechanism of muscle contraction. (or) Describe the chemistry and physiological role of posterior pituitary harmones. 3.Write an account of macro elements in human nutrition. (or) Define BMR.Discuss the factors effecting the BMR. 4.Describe the structure,biological and deficiency disorders of vitamin A. (or) Explain the kwashiorkar,Marasmus diseases of malnutrition and add a note on biological values of proteins.

Section B Answer any FIVE of the following.


5.Vitamin E.
6. Parathyroid harmone. 7.SDA. 8.Cardiac factors controlling blood pressure. 9.Role of essentinl fattyacids in human nutrition. 10.Composition of blood. 11.Obesity and starvation. 12.Signal transduction of insulin.

5x5=25Marks

Section C Answer any five of the following questions.


13.Gastric juice. 14.Coagulation. 15.ADH 16.Balanced diet. 17.Contractile proteins. 18.RDA. 19.Vitamin- B12 20.Neurotransmitter.

5x2=10Marks

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III B.Sc; BIOCHEMISTRY-PAPER-IV V SEMESTER MODELQUESTION PAPER 2011-12 (Microbiology and Molecularbiology)

Time:3hrs Section-A Answer all questions

Maximum marks:75 4x10=40 Marks

1.Discuss different growth media for bacterial cultures and add a note on batch culture. (or) Explain the bacterial growth curve and kinetics. 2.Describe the lytic and lysogenic cycles of -phase. (or) Describe gram staining process in detail. 3.Describe the m-RNA synthesis in bacteria. (or) Write the experimental proof for the semi-conservative mode of replication 4.Describe the experiments which proves DNA as a genetic material. (or) Explain the post transcriptional modifications of eukaryotic m-RNA and add a note on inhibitors of transcription

Section-B Answer ANY FIVE questions


5.Retro virus-HIV. 6.Industrial uses of yeast. 7.Structure and composition of viruses. 8.Isolation and cultivation of bacteria. 9.DNA polymerases. 10.Bidirectional mode of replication. 11.Meselson and stahs experiment. 12.Eukaryotic RNA polymerase.

5X5=25 Marks

Section-C Answer ANY FIVE questions


13.Selective media. 14.Aspergillus niger. 15. Virus. 16.Synchronous growth. 17.Gene. 18.Topoisomerases 19.Core enzyme. 20.Okazaki fragments.

5X2=10Marks

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III B.Sc; BIOCHEMISTRY-PAPER-III


VI SEMESTER MODEL QUESTION PAPER 2011-12 (Clinical biochemistry and immunology)

Time:3hrs Section A Answer ALL the questions.

Maximum marks:75 4X10=40Marks

1.Discuss the biochemical parameters for the differential diagnosis of jaundice. (Or) Explain the process of urine formation. 2.Describe the biochemical tests for diagnosis of heart diseases. (or) Explain diabetes mellitus and its types. 3.What is immunity?explain humeral immunity in detail. (or) Describe Ag-Ab reactions. 4.Describe the hybridoma technology of monoclonal antibodies. (or) What is hypersensitivity and add a note on fundamentals of graft rejection and MHC proteins .

Section B Answer anyFIVE questions


5.Clonal selection theory. 6.Serum enzyme in liver diseases. 7.Nephron structure. 8.GTT. 9.Recombinent and peptide vaccines. 10.Structure of Ig G. 11.ELISA. 12.Sickel cell anemia.

5X5=25 Marks

Section C Answer any five of the following questions


13.Fatty liver. 14.C-reactive protein. 15.Thalassemias. 16.Haptons. 17.RIA. 18.Glycosuria. 19.Secondary immune response. 20.Epitopes. *************

5x2=10Marks

III B.Sc; BIOCHEMISTRY-PAPER-IV


Time:3hrs VI SEMESTER MODELQUESTION PAPER 2011-12 (Regulation of gene expression-Recombinent-DNA Technology) Maximum marks:75

Section A Answer all questions 4x10=40Marks

1.Describe the process of protein synthesis. (or) What is genetic code and explain the properties of genetic code. 2.Describe the tryptophan operon concept in detail. (or) Explain the post-translation modifications and add anote on inhibitors of protein synthesis. 3.What is vector?Explain different types of vectors. (or) Construct the C-DNA genomic libraries. 4.Write the principle and applications of PCR technology. (or) Describe protein biological dababare.

Section B Answer any FIVE of the following


5.Wobble hypothesis. 6.Activation of amino acids. 7.Lac-operon. 8.Sangers dideoxy method of sequencing. 9.Souther blotting. 10.Production of insulin by gene cloning. 11.Sequency alinments. 12.Restriction endo nucleases.

5X5=25Marks

Section C Answer any five of the following


13.Operon. 14.Edible vaccines. 15.Attenuation. 16.Gene bank 17.HRT 18.Restriction mapping. 19.Expression vector. 20.Human growth hormone. *******

5x2=10Marks