Subject : M. Sc. BIOCHEMISTRY
Department of Biochemistry
Semester wise distribution of Courses and Credits
SEMESTER - I
BCM 101 : Cell Biology and Physiology
BCM 102 : Bioanalytical Techniques
BCM 103 : Methods in Molecular Biology
BCM 104M : Biomolecules & Microbial Biochemistry (for students of other PG programmes)
Minor Elective (for Biochemistry students)
BCM 105 : Practical: Bioorganic Preparations
BCM 106 : Practical: Analytical Biochemistry
SEMESTER – II
BCM 201 : Bioenergetics and Metabolism I
BCM 202 : Metabolism II
BCM 203 : Immunology
BCM 204M : Nutritional Biochemistry (for students of other PG programmes)
Minor Elective (for Biochemistry students)
BCM 205 Practical: Bioanalytical Techniques
BCM 206 Practical: Microbiology and Immunology
BCM 207 : Assignment based Seminar – I
SEMESTER – III
BCM 301 : Enzymology
BCM 302 : Plant Biochemistry
BCM 303 : Clinical Biochemistry
BCM 304M : Neurobiochemistry (for Biochemistry students only)
BCM 305 : Practical: Enzymology
BCM 306 : Practical: Enzyme Technology
BCM 307 : Assignment based Seminar - II
SEMESTER – IV
BCM 401 : Molecular Biology
BCM 402 : Outlines of Biotechnology
BCM 403 : Practical: Biochemical Preparations
BCM 404 : Practical: Clinical Biochemistry
BCM 405 : Assignment based Seminar - III
BCM 406 : Project Work Including Presentation, Comprehensive viva
SEMESTER – I
BCM 101: CELL BIOLOGY AND PHYSIOLOGY (Credits – 4)
1. Cell Biology - Cell classification, cell variability (size, shape, complexity, functions). Structural organization of prokaryotic and eukaryotic cells. The ultra structure of nucleus, mitochondria, endoplasmic reticulum (rough and smooth), Golgi apparatus, lysosomes & peroxisomes and their functions. The cytoskeleton – microtubules and microfilaments. Cell movement and chemotaxis.
2. Blood - Composition and functions of plasma, erythrocytes including Hb, Leucocytes and thrombocytes, plasma proteins. Blood Coagulation – mechanism and regulation. Transfer of blood gases – Oxygen and carbon dioxide, role of 2,3-diphosphoglycerate, Bohr effect and chloride shift.
3. Digestive system – Composition, functions and regulation of saliva, gastric, pancreatic, intestinal and bile secretions. Digestion and absorption of carbohydrates, lipids, proteins, & nucleic acids.
4. Respiration – Air passages and lung structure, pulmonary volumes, alveolar surface tension, work of breathing and its regulation.
5. Endocrine system – Secretion and functions of hormones of thyroid, pituitary and gonads. Role of hormones in reproduction. Mechanism of action of hormones.
6. Excretory system – Structure of nephron, glomerular filtration, tubular reabsorption of glucose, water and electrolytes. Tubular secretion. Homeostatic regulation of water and electrolytes, Acid-base balance.
BCM 102: BIOANALYTICAL TECHNIQUES (Credits – 4)
1. Spectroscopy - Concepts of spectroscopy, Laws of photometry. Beer-Lambert’s law, Principles and applications of colorimetry. Visible and UV spectroscopy, ORD, CD, X-ray diffraction, X-ray absorption and NMR.
2. Chromatography – Principles and applications of paper, thin layer, ion exchange, affinity, gel permeation, adsorption and partition chromatography. HPLC and FPLC.
3. Centrifugation – Principle of centrifugation, concepts of RCF, different types of instruments and rotors, preparative, differential and density gradient centrifugation, analytical ultra-centrifugation, determination of molecular weights and other applications, subcellular fractionation.
4. Electrophoretic techniques – Principles of electrophoretic separation. Types of electrophoresis including paper, cellulose, acetate/nitrate and gel. Electroporation, Pulse field gel electrophoresis.
5. Electron microscopy – Transmission and scanning, freeze fracture techniques, specific staining of biological materials.
6. Viscosity – Viscosity of macromolecules, relationship with conformational changes.
BCM 103: METHODS IN MOLECULAR BIOLOGY (Credits – 4)
1. Recombinant DNA methods – Features of commonly used vectors, strategies for cloning in various vectors and Identification of bacterial colonies containing recombinant plasmids, and bacteriophage vectors. Restriction enzymes.
2. Construction and analysis of c-DNA and genomic libraries - Protocols and strategies for c-DNA cloning, analysis of genomic DNA by southern hybridization, amplification of DNA by the polymerase chain reaction, preparation of radio-labeled DNA and RNA probes, synthetic oligonucleotide probes, expression of cloned genes in cultured cells, screening expression with antibodies and oligonucleotides.
3. DNA sequencing – Rapid DNA sequencing methods; Maxam-Gilbert technique, Sanger’s Dideoxynucleotide sequencing, gene walking, foot printing, RNA sequencing.
4. Application of recombinant technology – production of insulin, drug, vaccines, diagnostic probe of genetic diseases. Gene therapy.
5. Chromatin – Heterochromatin, euchromatin. Histone and non-histone proteins, general properties of histone, packing density, nucleosomes, size, variable linkers, solenoid structure, packaging of DNA, satellite DNA.
6. Genes – Prokaryotic and eukaryotic genes, pseudogenes, split genes, super gene family, transposons, Cvalue paradox. Reassociation kinetics.
7. Mutation – Types of mutations, mechanism of mutation, mutagenic agents. DNA repair: UV repair system in E. coli.
BCM 104M : BIOMOLECULES AND MICROBIAL BIOCHEMISTRY (Credits – 3)
(Minor Elective)
Bio-molecules:
1. Carbohydrates – Structure, reactions and functions of monosaccharides, disaccharides polysaccharides and complex carbohydrates; amino sugars, proteoglycans and glycoproteins.
2. Lipids - Classification, structure, properties and functions of fatty acids, essential fatty acids, fats, phospholipids, sphingolipids, cerebrosides, steroids, bile acids, prostaglandins and lipoproteins.
3. Nucleic acids - Structure and function of nucleotides. Primary, secondary and tertiary structure of nucleic acids, DNA forms and conformations.
4. Proteins – Primary, Secondary, Tertiary and Quaternary structures of proteins.
5. Enzymes - Historical perspective, general characteristics, nomenclature, Enzyme classification (specific examples), and Enzyme assays.
Microbial Biochemistry:
6. Morphology and Structure of bacteria, gram positive and gram negative organisms. Microscopy (Bright field, Dark field, Phase contrast and Fluorescence microscopy), sterilization: physical and chemical methods. Nutritional requirements and growth characteristics of bacteria, media for growing bacteria.
7. Bacterial toxins – Classification, structure and mode of action of bacterial protein toxins, enterotoxins.
8. Viruses – General structure, properties and classification. Virions, prions, lytic cycle, lysogeny, plasmid.
BCM 105 : PRACTICAL : BIOORGANIC PREPARATIONS (Credits – 3)
Organic Preparations of:
1. ρ-nitrophenyl acetate
2. An aromatic alpha- and beta-glucoside starting with glucose
3. Dinitrophenyl hydrazone of ascorbic acid or any other ketone
4. Dinitrophenyl derivative of an amino acid
5. Fractionation of egg proteins and its quantification
6. Isolation of casein from milk and its quantification
BCM 106 : PRACTICAL : ANALYTICAL BIOCHEMISTRY (Credits – 3)
1. Carbohydrates: Qualitative analysis, quantitation of glucose and ribose.
2. Amino acids and proteins: Qualitative analysis, quantitation of proteins and amino acids.
3. Quantitation of free and bound phosphate.
4. Quantitation of vitamin C.
5. Fats: Acid number, saponification and iodine values.
SEMESTER – II
BCM 201 : BIOENERGETICS AND METABOLISM I (Credits – 4)
1. Bioenergetics – Concept of free energy, standard free energy, determination of ΔG for a reaction. Relationship between equilibrium constant and standard free energy change, biological standard state & standard free energy change in coupled reactions. Biological oxidation-reduction reactions, redox potentials, relation between standard reduction potentials and free energy change (derivations and numericals included). High energy phosphate compounds – introduction, phosphate group transfer, free energy of hydrolysis of ATP and sugar phosphates alongwith reasons for high ΔG. Energy charge.
2. Intermediary Metabolism – Approaches for studying metabolism.
3. Coenzymes and Cofactors – Role and mechanism of action of NAD+/NADP+, FAD, lipoic acid, thiamine pyrophosphate, tetrahydrofolate, biotin, pyridoxal phosphate, B12 coenzymes and metal ions with specific examples.
4. Carbohydrates – Glycolysis, various forms of fermentations in micro-organisms, citric acid cycle, its function in energy generation and biosynthesis of energy rich bond, pentose phosphate pathway and its regulation. Gluconeogenesis, glycogenesis and glycogenolysis, glyoxylate and Gamma aminobutyrate shunt pathways, Cori cycle, anaplerotic reactions, Entner-Doudoroff pathway, glucuronate pathway. Metabolism of disaccharides. Hormonal regulation of carbohydrate metabolism. Energetics of metabolic cycle.
5. Amino Acids – General reactions of amino acid metabolism - Transamination, decarboxylation, oxidative and non-oxidative deamination of amino acids. Special metabolism of methionine, histidine, phenylalanine, tyrosine, tryptophan, lysine, valine, leucine, isoleucine and polyamines. Urea cycle and its regulation.
BCM 202 : METABOLISM II (Credits – 4)
1. Lipids – Introduction, hydrolysis of tri-acylglycerols, α-, ß- and ω- oxidation of fatty acids. Oxidation of odd numbered fatty acids – fate of propionate, role of carnitine, degradation of complex lipids. Fatty acid biosynthesis, Acetyl CoA carboxylase, fatty acid synthase, ACP structure and function, Lipid biosynthesis, biosynthetic pathway for tri-acylglycerols, phosphoglycerides, sphingomyelin and prostaglandins. Metabolism of cholesterol and its regulation. Energetics of fatty acid cycle.
2. Nucleotides – Biosynthesis and degradation of purine and pyrimidine nucleotides and its regulation. Purine salvage pathway. Role of ribonucleotide reductase. Biosynthesis of deoxyribonucleotides and polynucleotides including inhibitors of nucleic acid biosynthesis.
3. Biosynthesis of vitamins – Ascorbic acid, thiamine, pantothenic acid and folic acid.
4. Biochemistry of biological nitrogen fixation.
5. Porphyrins – Biosynthesis & degradation of porphyrins. Production of bile pigments.
6. Plant Hormones – Growth regulating substances and their mode of action, molecular effects of auxin in regulation of cell extension, effects of gibberellic, abscisic acids and cytokinins in the regulation of seed dormancy, germination, growth and development.
BCM 203 : IMMUNOLOGY (Credits – 4)
1. Introduction to immune system – Innate and acquired immunity. Structure and functions of primary and secondary lymphoid organs.
2. Cells involved in immune responses – Lymphoid cells (B-lymphocytes, T-lymphocytes and Null cells), mononuclear cells (phagocytic cells and their killing mechanisms), granulocytic cells (neutrophils, eosinophils and basophils), mast cells and dendritic cell.
3. Nature of antigen and antibody – Immunogenicity vs antigenicity, factors influencing immunogenicity, epitopes, haptens, adjuvants and mitogens. Classification, fine structure and functions of immunoglobulins, antigenic determinants on immunoglobulins, isotypic, allotypic and ideotypic variants.
4. Generation of Diversity in Immune system – Clonal selection theory - concept of antigen specific receptor. Organization of immunoglobulin genes: generation of antibody diversity, T-cell receptor diversity.
5. Immune effector Mechanisms – Kinetics of primary and secondary immune responses, complement activation and its biological consequences, cytokines and co-stimulatory molecules: role in immune responses, Antigen processing and presentation. Cell signaling – Role of MAP kinases.
6. Major histocompatibility complex (MHC) genes and products – Polymorphism of MHC genes, role of MHC antigens in immune responses, MHC antigens in transplantation.
7. Measurement of antigen–antibody interactions – Agglutination, precipitation and opsonization, gel diffusion (Ouchterlony double immunodiffusion and Mancini’s Radial immunodiffusion), immunoblotting, RIA, ELISA and ELISPOT.
8. Tolerance vs activation of immune system – Immune tolerance, hypersensitivity (Types I, II, III, IV).
9. Disorders of immune system – Autoimmunity, congenital immunodeficiencies, acquired immunodeficiencies.
BCM 204M : NUTRITIONAL BIOCHEMISTRY (Credits – 3)
(Minor Elective)
1. Basic concepts - Function of nutrients. Measurement of the fuel values of foods. Direct and indirect calorimetry. Basal metabolic rate; factors affecting BMR, measurement and calculation of BMR. Measurement of energy requirements. Specific dynamic action of proteins. Recommended dietary allowances.
2. Elements of nutrition – Dietary requirement of carbohydrates, lipids and proteins. Biological value of proteins. Concepts of protein quality. Protein sparing action of carbohydrates and fats. Essential amino acids, essential fatty acids and their physiological functions.
3. Vitamins – Dietary sources, biochemical functions, requirements and deficiency diseases associated with vitamin B complex, C and A, D, E & K vitamins.
4. Minerals – Nutritional significance of dietary calcium, phosphorus, magnesium, iron, iodine, zinc and copper.
5. Malnutrition – Prevention of malnutrition, improvement of diets.
BCM 205 : PRACTICAL : BIOANALYTICAL TECHNIQUES (Credits – 3)
1. Titration of a weak acid using a pH meter, preparation of buffers
2. Verification of Beer-Lambert’s law and estimation of absorption coefficient
3. Paper chromatography – Separation of amino acids and carbohydrates in a mixture
4. Thin layer chromatography of fatty acids.
5. Column chromatography – Separation of a mixture of protein and salt using Sephadex column
6. Electrophoresis
BCM 206 : PRACTICAL : MICROBIOLOGY AND IMMUNOLOGY (Credits – 3)
1. Preparation of stains and reagents
2. Preparation of various culture media
3. Preparation of broth and slants
4. Sterilization of culture media by autoclave method
5. Sterilization of glassware by hot air oven
6. Isolation and propagation of bacteria
7. Staining of bacteria – Simple staining, differential staining, staining of spores and capsules
8. Determination of growth curve of bacteria
9. Biochemical tests and motility for the identification of bacteria
10. Precipitin reaction by double immunodiffusion and radial immunodiffusion (Ouchterlony and Mancini’s methods)
11. Detection of antibodies or antigen by ELISA (Indirect and Sandwich ELISA)
12. Detection of antigens by immunoblotting technique
BCM 207 : ASSIGNMENT BASED SEMINAR – I (Credits – 2)
SEMESTER – III
BCM 301 : ENZYMOLOGY (Credits – 4)
1. Introduction – IUB enzyme classification (specific examples), enzyme specificity, methods for isolation, purification and characterization of enzymes, tests for homogeneity of enzyme preparation.
2. Kinetics of enzyme action – Concept of ES complex, active site, specificity, derivation of Michaelis- Menten equation for uni- substrate reactions. Different plots for the determination of Km & Vmax and their physiological significances. Importance of Kcat/Km. Kinetics of zero & first order reactions. Significance and evaluation of energy of activation. Michaelis – pH functions and their significance. Classification of multi-substrate reactions with examples of each class. Derivation of the rate of expression for Ping Pong, random & ordered Bi-Bi mechanisms. Use of initial velocity, inhibition and exchange studies to differentiate between multi-substrate reaction mechanisms. Reversible and irreversible inhibition.
Competitive, non-competitive, uncompetitive, linear-mixed type inhibitions and their kinetics, determination of Ki and numerical based on these. Suicide inhibitor.
3. Mechanism of Enzyme Action – Acid-base catalysis, covalent catalysis, proximity, orientation effect. Strain and distortion theory. Chemical modification of active site groups. Site directed mutagenesis of enzymes. Mechanism of action of chymotrypsin, lysozyme, glyceraldehyde 3-phosphate dehydrogenase, aldolase, carboxypeptidase, triose phosphate isomerase and alcohol dehydrogenase.
4. Enzyme Regulation – General mechanisms of enzyme regulation, product inhibition. Reversible (glutamine synthase & phosphorylase) and irreversible (proteases) covalent modification of enzymes. Mono-cyclic and multi-cyclic cascade systems with specific examples. Feed back inhibition and feed forward stimulation. Allosteric enzymes, qualitative description of “concerted” & “sequential” models for allosteric enzymes. Half site reactivity, positive and negative co-operativity with special reference to aspartate transcarbamoylase and phosphofructokinase. Protein-ligand binding measurement, analysis of binding isotherms, Hill and Scatchard plots.
5. Multienzyme system – Occurrence, isolation and their properties: Mechanism of action and regulation of pyruvate dehydrogenase complex. Enzyme-enzyme interaction, multiple forms of enzymes with special reference to lactate dehydrogenase.
BCM 302 : PLANT BIOCHEMISTRY (Credits – 4)
1. Electron transport system in plants - Oxidative phosphorylation, mitochondrial respiratory complexes, order and organization of electron carriers, electrochemical gradient, chemiosmotic theory, ATP synthase and mechanism of ATP synthesis.
2. Nitrate assimilation - Structural features of nitrate reductase and nitrite reductase, incorporation of ammonia into organic compounds, regulation of nitrate assimilation.
3. Photosynthesis – Photosynthetic apparatus, pigments of photosynthesis, role of carotenoids, photosystems I and II, their location; Hill reaction, photosynthetic electron transport and generation of NADPH & ATP, cyclic and non-cyclic photo-phosphorylations, complexes associated with thylakoid membranes; light harvesting complexes, path of carbon in photosynthesis – C3 and C4 pathway of carbon reduction and its regulation, Photorespiration.
4. Special features of secondary plant metabolism - Terpenes (classification, biosynthesis), lignin, tannins, pigments, phytochrome, waxes, alkaloids, biosynthesis of nicotine, functions of alkaloids, cell wall components.
5. Toxins of plant origin – Mycotoxins, phytohemagglutinins, lathyrogens, nitriles, protease inhibitors, protein toxins.
6. Stress metabolism in plants - Environmental stresses, salinity, water stress, heat, chilling, anaerobiosis, pathogenesis, heavy metals, radiations and their impact on plant growth and metabolism, criteria of stress tolerance.
7. Antioxidative defence system in plants – Reactive oxygen species and their generation, enzymic and non-enzymic components of antioxidative defense mechanism.
BCM 303: CLINICAL BIOCHEMISTRY (Credits – 4)
1. Disorders of Carbohydrate Metabolism - Diabetes mellitus, glucose and galactose tolerance tests, sugar levels in blood, renal threshold for glucose, factors influencing blood glucose level, glycogen storage diseases, pentosuria, galactosemia.
2. Disorders of Lipids – Plasma lipoproteins, cholesterol, triglycerides and phospholipids in health and disease, hyperlipidemia, hyperlipoproteinemia, Gaucher’s disease, Tay-Sach’s and Niemann-Pick disease, ketone bodies, Abetalipoproteinemia.
3. Inborn Errors of metabolism – Phenylketonuria, alkaptonuria, albinism, tyrosinosis, maple syrup urine disease, Lesch-Nyhan syndrome, sickle cell anemia, histidinemia.
4. Digestive diseases – Maldigestion, malabsorption, creatorrhoea, diarrhoea and steatorrhoea.
5. Disorders of liver and kidney – Jaundice, fatty liver, normal and abnormal functions of liver and kidney. Inulin and urea clearance.
6. Electrolytes and acid-base balance – Regulation of electrolyte content of body fluids and maintenance of pH, reabsorption of electrolytes.
7. Diagnostic Enzymes – Enzymes in health and diseases. Biochemical diagnosis of diseases by enzyme assays – SGOT, SGPT, CPK, cholinesterase, LDH.
8. Abnormalities in Nitrogen Metabolism – Uremia, hyperuricemia, porphyria and factors affecting nitrogen balance.
9. Blood Clotting – Disturbances in blood clotting mechanism – hemorrhagic disorders – hemophilia, von Willebrand’s disease, purpura, Rendu-Osler-Werber disease, thrombotic thrombocytopenic purpura, disseminated intravascular coagulation, acquired prothrombin complex disorders, circulating anticoagulants.
10. Cancer – Cellular differentiation, carcinogens and cancer therapy.
BCM 304M : NEUROBIOCHEMISTRY (Credits – 3)
(Minor Elective)
1. Muscle Biochemistry – Skeletal muscle structure. Actin, myosin, tropomyosin, troponin. Molecular mechanism of contraction. Functional classification of skeletal muscle fibers. Twitch. The motor unit. Role of calmodulin.
2. Neuromorphology – Organisation of neuron, dendrites and axons. Glial cells – astrocytes, oligodendrocytes, ependymal cells, Schwan cells. Nerve fiber types and functions.
3. Neurophysiology – Generation and conduction of monophasic action potential, saltatory conduction. Synaptic transmission, Neurotransmitters and their action. Blood Brain CSF barrier – Characteristics.
4. Transport across membranes – Types of transport (simple diffusion, passive-facilitated diffusion), active transport – primary and secondary group translocation, transport ATPases, transport by vesicle formation.
5. Neurological disorders – Headache, facial pain, migraine, epilepsy, multiple sclerosis, Myasthenia Gravis.
BCM 305 : PRACTICAL : ENZYMOLOGY (Credits – 3)
1. Assay of enzyme activity
2. Isolation and purification of urease.
3. Time course of enzymatic reaction.
4. Influence of substrate concentration on the rate of enzymatic reaction.
5. Effect of pH and temperature on the rate of enzyme reaction.
6. Specificity of enzyme action.
7. Inhibition of enzyme activity. Determination of Ki values.
BCM 306 : PRACTICAL : ENZYME TECHNOLOGY (Credits – 3)
1. Molecular weight determination of enzyme by gel filtration.
2. Isozyme detection.
3. Immobilization studies:
a) Preparation of urease entrapped in alginate beads and determination of percent entrapment.
b) Study of the kinetics of the rate of urea hydrolysis by urease entrapped alginate beads.
c) Study of reusability and storage stability of urease entrapped alginate beads.
d) Immobilization of urease by covalent attachment to solid support.
BCM 307: ASSIGNMENT BASED SEMINAR – II (Credit – 1)
SEMESTER – IV
BCM 401: MOLECULAR BIOLOGY (Credits – 4)
1. DNA Replication - Mechanism of replication, the replicons, origin, primosome and replisomes, properties of prokaryotic and eukaryotic DNA polymerases, synthesis of leading and lagging strands, difference between prokaryotic and eukaryotic replication.
2. Mechanism of Transcription – Prokaryotic transcription, promoters, properties of bacterial RNA polymerase; initiation, elongation and termination. Eukaryotic transcription, promoters, enhancers, factors & properties of RNA polymerase I, II, & III. Reverse transcription. Inhibitors of transcription.
3. Post transcriptional Processing - Maturation of rRNA, mRNA and tRNA; RNA splicing, introns and exons, consensus sequence function. Poly A tail, 5’ capping.
4. Recombination – General recombination, site specific recombination and replicative recombination.
5. Genetic Code – Deciphering of the codons, reading frame of a sequence, Start/stop codons, degeneracy of the genetic code, Wobble hypothesis, variations to the standard genetic code.
6. Translation in Pro- and Eukaryotes – Ribosomes, structure, functional domain and subunit assembly, cell free protein synthesis, direction of protein synthesis (Dintzis experiment), adaptor role of tRNA, formation of initiation complex, chain elongation, translocation & termination, and role of respective factors involved therein. Inhibitors of protein biosynthesis. Comparison of protein biosynthesis in prokaryotes with eukaryotes. Post Translational processing – Proteolytic cleavage, covalent modifications, glycosylation of proteins, disulfide bond formation.
7. Protein Localization – Co- and post-translational protein traslocation; chaperones and protein folding, signal sequences, translocons, leader sequences.
8. Regulation of Transcription and Translation - Positive and negative control, Repressor & Inducer, concept of operon, lac-, ara-, trp-operons, attenuation, catabolite repression, autogenous regulation, lytic cycle of bacteriophage, stringent response of rRNA synthesis. Hormonal control, transcription factors, steroid receptors. DNA binding motifs in pro- & eukaryotes, helix-turn-helix, zinc fingers, leucine zippers/b zip, helix-loop-helix motifs.
BCM 402: OUTLINES OF BIOTECHNOLOGY (Credits – 4)
1. Plant genetic engineering - Prospects of improving crop productivity, gene isolation, gene transfer systems, Ti plasmid, plant virus vectors, electroporation, microinjection, microprojectile technology, gene expression, regeneration. Application in relation to protein quality, photosynthetic efficacy, nitrogen fixation efficiency and resistance to environmental stresses.
2. Tissue culture – Plant tissue culture, anther and pollen culture, protoplast culture, protoplast fusion, embryo rescue, animal cell lines and organ culture.
3. Transgenic plants and animals – Advances in producing transgenics, transgenic animals.
4. Fermentation technology – Fermentors, general design of fermentor, fermentation processes, production of alcohols, antibiotics, steroids and enzymes; biotransformation, biomass & production of single cell protein.
5. Hybridoma technology – Monoclonal antibodies, selection of hybrids, hybridomas, purification and application of monoclonal antibodies.
6. Xenobiotic metabolism – Biodegradation, detoxification of xenobiotics by micro-organisms, biodegradation of hydrocarbons, pesticides, surfactants, polyaromatic hydrocarbons, dyes; role of cytochrome P450 in detoxification.
7. Proteomics – Genome to Proteome, steps and tools for proteome analysis, 2 D-Electrophoresis, BNPAGE.
8. Enzyme Technology - Large scale production of enzymes, enzyme reactors, immobilization of enzymes by chemical and physical methods. Effect of partition on kinetics and on changes in pH and hydrophobicity. Applications: synthetic organic chemistry, industry, food technology, medicines. Synzymes, enzyme electrodes and biosensors. Enzyme Engineering.
BCM 403: PRACTICAL : BIOCHEMICAL PREPARATIONS (Credits – 3)
1. Fractionation of cell organelles from liver and plant tissues.
2. Isolation of NAD+ from brewer’s yeast.
3. Isolation and estimation of RNA and DNA from yeast, liver, and plants.
4. Extraction, separation and determination of absorption spectra of plant pigments.
5. Isolation and estimation of serum cholesterol.
6. Gel electrophoresis of serum proteins, SDS-PAGE of proteins.
BCM 404: PRACTICAL : CLINICAL BIOCHEMISTRY (Credits – 3)
1. Determination of α-amylase of saliva.
2. Qualitative and quantitative analysis of following in urine:
(i) Urea
(ii) Uric acid
(iii) Glucose
(iv) Proteins
(v) Bence-Jones proteins
(vi) Cl-, PO33-, Ca2+
3. Estimation of hemoglobin by canomethemoglobin
4. Quantification of serum proteins
5. Determination of A/G ratio in serum
6. Estimation of serum glucose, creatinine and uric acid.
7. Assay of serum enzymes : alkaline phosphatase, SGOT, SGPT
BCM 405: ASSIGNMENT BASED SEMINAR – III (Credits – 2)
BCM 406: PROJECT WORK INCLUDING PRESENTATION (Credits – 8 )
COMPRESENSIVE VIVA
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