Model Curriculum BIOCHEMISTRY (UG courses)
May 2008 A.P. State Council of Higher Education
Biochemistry 2 of 8
SUBJECT COMMITTEE 1. Prof. D. Siva Prasad Department of Biochemistry, Andhra University, Visakhapatnam. 2. Prof. M S K Prasad Department of Biochemistry, Kakatiya University, Warangal. 3. Prof. K. Thyagaraju Department of Biochemistry, Sri Venkateswara University, Tirupati. 4. Prof. B. Sashidhar Rao Department of Biochemistry, Osmania University, Hyderabad. 5. Prof. P.V.V. Satyanarayana, Department of Biochemistry, Acharya Nagarjuna University, Nagarjuna Nagar, Guntur Dist. 6. Prof. D. Sarala Kumari Department of Biochemistry, Sri Krishnadevaraya University, Anantapur. 7. Dr. G. Sudhakar Reddy Govt. Degree College, Piler, Chittoor Dist. 8. Dr. G. Seshagiri Rao Department of Biochemistry, Andhra University, Visakhapatnam. 9. Prof. S. Sanjeevi Rao Department of Biochemistry, Andhra Medical College, Visakhapatnam. 10. Prof. P. V. Subba Rao General Manager, Divis Laboratories Ltd. Phippada, Annavaram P, Visakhapatnam Dist.
Coordinator
Biochemistry 3 of 8
MODEL CURRICULUM B.Sc. Courses (Structure) First year: S.no.
Subject
Hrs per week
1. 2. 3. 4. 5. 6. 7. 8. 9. 10.
English language including communication skills Second language Core1-I Core2-I Core3-I Core1-lab I Core2-lab I Core3-lab I Foundation course Computer skills Total
S.no.
Subject
1. 2. 3. 4. 5. 6. 7. 8. 9. 10.
English language including communication skills Second language Core1-II Core2-II Core3-II Core1-lab II Core2-lab II Core3-lab II Environmental studies Computer skills Total
S.no.
Subject
1. 2. 3. 4. 5. 6. 7. 8. 9. 10. 11. 12. 13.
Core1-III Core1-IV Core2-III Core2-IV Core3-III Core3-IV Core1-lab III Core1-lab IV Core2-lab III Core2-lab IV Core3-lab III Core3-lab IV Foundation course
6 4 4 4 4 3 3 3 3 2 36
Second year: Hrs per week 6 4 4 4 4 3 3 3 4 2 37
Third year: Hrs per week
Total
3 3 3 3 3 3 3 3 3 3 3 3 3 39
Biochemistry 4 of 8
A.P.State Council of Higher Education, Hyderabad Model Curriculum Biochemistry Course Structure, Scheme of Instruction and Examination
Year
I
II
III
Theory / Practical Paper No.
Title
Work load / Hours per Week
Exam Duration Hours
Marks
Theory Paper I
Biomolecules and Enzymology
4
3
100
Practicals Paper I
Qualitative Analysis and Enzymology
3
3
50
Theory Paper II
Metabolism and Biochemical Techniques
4
3
100
Practicals Paper II
Quantitative Analysis and Biochemical Techniques
3
3
50
Theory Paper III
Physiology, Clinical Biochemistry and Immunology
3
3
100
Theory Paper IV
Microbiology and Molecular Biology
3
3
100
Practicals Paper III
Nutritional and Clinical Biochemistry
3
3
50
Practicals Paper IV
Microbiology and Molecular Biology
3
3
50
Note: Foundation Course: (i)
1st Year: Mathematics for Biology Students / Biology for Mathematics Students
(ii) 2nd Year: Environmental Studies. (iii) 3rd Year: Computational Science (Biostatistics, Bioinformatics).
Biochemistry 5 of 8
Model Curriculum Biochemistry Course Structure First Year
Marks
Theory – Paper-I: Biomolecules and Enzymology Unit-I
100
: Carbohydrates and Lipids
Unit-II : Amino acids, Peptides and Proteins Unit-III : Nucleic acids and Porphyrins Unit-IV : Enzymology Practicals – Paper-I: Qualitative Analysis and Enzymology Second Year
Marks
Theory – Paper-II: Metabolism and Biochemical Techniques Unit-I
50
100
: Bioenergetics and Biological Oxidations
Unit-II : Carbohydrate and Lipid Metabolism Unit-III : Metabolism of Nitrogen Compounds Unit-IV : Biochemical Techniques Practicals – Paper-II: Quantitative Analysis and Biochemical Techniques
50
Marks
Third Year
Theory – Paper-III: Physiology, Clinical Biochemistry and Immunology Unit-I
100
: Physiology
Unit-II : Nutritional Biochemistry Unit-III : Clinical Biochemistry Unit-IV : Immunology Theory – Paper-IV: Microbiology and Molecular Biology Unit-I
100
: Microbiology
Unit-II : DNA Replication and Transcription Unit-III : Protein Synthesis and Regulation of Gene Expression Unit-IV : Recombinant-DNA Technology Practicals – Paper-III: Nutritional and Clinical Biochemistry
50
Practicals – Paper-IV: Microbiology and Molecular Biology
50
Note: Foundation Course:
(i) (ii) (iii)
1st Year: Mathematics for Biology Students / Biology for Mathematics Students 2nd Year: Environmental Studies. 3rd Year: Computational Science (Biostatistics, Bioinformatics).
Biochemistry 6 of 8 120 hrs
2nd Year Theory – Paper-II: Metabolism and Biochemical Techniques Unit- I : Bioenergetics and Biological Oxidations
(4 hrs/week)
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 (ε, (ε’o) of some biochemically important half reactions.
εo, ε’o). Standard reduction potential
Ultra structure of mitochondria. Electron transport chain and carriers involved. Oxidative phosphorylation, theories of oxidative phosphorylation- Mitchell’s chemiosmotic theory. Fo F1- 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 pyruvateformation 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, C4 Pathway. Catabolism of fatty acids (β- 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. 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 metabolismGout, Lesch- Nyhan syndrome. Biosynthesis and degradation of heme.
Biochemistry 7 of 8 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, ionexchange 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, β and γ- emitters, use of radioactive isotopes in biology.
Biochemistry 8 of 8 2nd Year Practical – Paper-II: Quantitative Analysis and Biochemical Techniques
90 hrs (3 hrs/week)
List of Experiments:
1. Estimation of amino acid by ninhydrin method. 2. Estimation of protein by Biuret method. 3. Estimation of protein by Lowry method. 4. Estimation of glucose by DNS method. 5. Estimation of glucose by Benedict’s titrimetric method. 6. Estimation of total carbohydrates by anthrone method. 7. Isolation of egg albumin from egg white. 8. Isolation of cholesterol from egg yolk. 9. Isolation of starch from potatoes. 10. Isolation of casein from milk. 11. Separation of amino acids by paper chromatography. 12. Determination of exchange capacity of resin by titrimetry. 13. Separation of serum proteins by paper electrophoresis. 14. Separation of plant pigments by TLC.