Dr. R.L. prasadSurendra Kumar2024-06-132024-06-131994https://krishikosh.egranth.ac.in/handle/1/5810210427The isolation and characterization of proteins of goat skeletal muscle were undertaken with a view to their molecular profile in regulation of muscle contraction through ATPase activity and losses due to proteolysis by artificial tenderizer of meat. The goat skeletal muscle myosin was isolated in pure form using different ionic strength, dissociation buffer and ammonium sulphate precipitation. The myosin contained myosin heavy chain (HC) and myosin light chain-1 (LC), myosin light chain-2 (LC) and myosin light chain-3 (LC) with 2 their molecular weights of 192.5, 23, 17.5 and 13.5 kDa respectively. The resolution of sarcoplasmic proteins into subunit components on SDS-PAGE showed the presence of enzymes and metallo proteins. The high molecular weight of unidentified proteins was present in band no.1-4. The molecular weight of 91 kDa appeared in band no.5 which was identified as phosphorylase B. The band no.6 was identified as phosphorylase B kinase with molecular weight of 77 kDa. Band no.7 was represented by AMP deaminase, phosphoglucose isomerase and pyruvate kinase with molecular weight of 62 kDa. Phosphoglycerate kinase and enclose appeared in band no.8 with molecular weight of 43 kDa. Band no.9 consisted of creatine phosphokinase, aldolase and lactic dehydrogenase having molecular weight of 34 kDa. Band no. 10 was identified as triose phosphate isomerase and phosphoglycerate mutase with molecular weight of 26 kDa.EnglishThesis