The document outlines the course structure for a Bachelor of Science in Clinical Biochemistry under a Choice Based Credit Scheme, detailing the courses and credits for each semester. It includes specific courses such as Biomolecules, Clinical Immunology, and Clinical Pathology, along with their respective practical components. Additionally, it provides an overview of the first semester's core course, including objectives, learning outcomes, and practical laboratory exercises.
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Clinical biochemistry
The document outlines the course structure for a Bachelor of Science in Clinical Biochemistry under a Choice Based Credit Scheme, detailing the courses and credits for each semester. It includes specific courses such as Biomolecules, Clinical Immunology, and Clinical Pathology, along with their respective practical components. Additionally, it provides an overview of the first semester's core course, including objectives, learning outcomes, and practical laboratory exercises.
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CHOICE BASED CREDIT SCHEME AT UNDER-GRADUATE LEVEL
COURSE STRUCTURE OF B. Sc. WITH CLINICAL BIOCHEMISTRY
SEM COURSE COURSE TITLE OF COURSE CREDITS
CODE TYPE THEORY PRACTICAL I CLB120C DSC-1 BIOMOLECULES- METABOLISM AND 4 2 RELATED DISORDERS II CLB220C DSC-2 CLINICAL IMMUNOLOGY AND 4 2 MICROBIOLOGY III CLB320C DSC-3 CELL AND MOLECULAR BIOLOGY 4 2 IV CLB420C DSC-4 ORGAN FUNCTION AND RELATED 4 2 DISORDERS VA CLB520DA DSE-1A CLINICAL BIOCHEMISTRY AND 4 2 OR ENZYMOLOGY VB CLB520DB DSE-1B CLINICAL HAEMATOLOGY 4 2 VIA CLB620DA DSE-2A CLINICAL PATHOLOGY 4 2 OR CLB620DB DSE-2B BIO-ANALYTICAL TECHNIQUES 4 2 VIB BACHELOR OF SCIENCE (GENERAL) 1st SEMESTER DISCIPLINE SPECIFIC COURSE (CORE) CLB120C: CLINICAL BIOCHEMISTRY: BIOMOLECULES- METABOLISM AND RELATED DISORDERS CREDITS: THEORY – 4, PRACTICAL – 2 THEORY (4 CREDITS: 60 HOURS) MAXIMUM MARKS: 60, MINIMUM MARKS: 24
Objectives and Expected Learning Outcomes:
To acquaint the students with basic understanding of the structure and properties of macromolecules that interact to maintain and perpetuate the living systems. Knowledge on the structure and function of different biomolecules would enable the students to consolidate their focus on understanding various metabolic pathways crucial for the sustenance of living systems.
UNIT-1 (15 Hours)
Chemistry of Carbohydrates: Definition, classification and structure of monosaccharides and important polysaccharides; Metabolism of Carbohydrates - Glycolysis, Krebs cycle, Pentose phosphate pathway, Gluconeogenesis, Glycogenesis, Glycogenolysis; Regulation of carbohydrate metabolism. Inborn errors of carbohydrate metabolism
UNIT-2 (15 Hours)
Chemistry of Amino acids and Proteins: Structure, classification, properties and functions; Peptide bond, secondary, tertiary, quaternary structure; Metabolism of Amino acid: Transamination, oxidative deamination, Urea cycle, Degradation of amino acids like tryptophan, tyrosine, methionine cysteine Inborn errors of amino acid metabolism
UNIT-3 (15 Hours)
Chemistry of Lipids: classification, structure, properties and functions of fatty acids, triacylglycerol, phospholipids, sterols, lipids with special biological functions. Lipid metabolism: Biosynthesis and degradation of saturated and unsaturated fatty acids, ketone bodies and cholesterol. Disorders of lipid metabolism
UNIT-4 (15 Hours)
Chemistry of Nucleic acids: structure and properties of purines and pyrimidine bases, nucleoside and nucleotides, conformation of nucleic acids, stability of nucleic acid structure.Nucleic Acid metabolism: Biosynthesis and degradation of purines and pyrimidines; Regulation of purines and pyrimidine biosynthesis, Disorders of purine / Pyrimidine metabolism.
1) Preparation of standard Buffers and determination of pH of a solution.
2) Principle, working and maintenance of pH meter and Weighing balance 3) Biochemical calculations – Molarity, Molality, Normality, percent solution 4) Qualitative tests for Carbohydrates – Molisch, Fehling’s, Benedict’s test 5) Qualitative tests for Proteins and Amino acids 6) Quantitative estimation of carbohydrates 7) Quantitative estimation of proteins by Lowry’s method