Conformational changes of myosin by gamma irradiation

Conformational and decompositional changes of bovine skeletal muscle myosin caused by gamma irradiation were studied for understanding the effects of irradiation treatment on myofibrillar proteins. Myosin solution and beef cu ts were irradiated 0, 1, 3, 5 and 10 kGy. Competitive indirect enzyme linke d immunosorbent assay (Ci-ELISA) showed that subunits of myosin were struct urally modified with different patterns. Binding abilities of antimyosin wh ole molecule and anti heavy meromyosin S-l IgG, which were produced from ra bbits, with irradiated myosin decreased in the same tendency depending upon the dose. Anti-light meromyosin IgG appeared to have the highest binding a bility at 3 kGy. Irradiated beef cuts (greater than or equal to 5 kGy) coul d be identified by Ci-ELISA. Myosin solution became increasingly turbid wit h increasing dose. Hydrophobicity of myosin solution also increased by irra diation. Electrophoretic patterns showed that the myosin heavy chain disapp eared and new bands were generated at higher molecular weight ranges. (C) 2 000 Elsevier Science Ltd. All rights reserved.