【摘要】 本文研究了白鲢鱼肌肉中肌原纤维结合型丝氨酸蛋白酶(myofibril-boundserineproteinase,MBSP)的作用。SDS-PAGE结果显示肌原纤维在55～60℃下加热后肌球蛋白重链有明显的分解现象。长时间加热也导致α-辅肌动蛋白,肌动蛋白和原肌球蛋白的分解。此结果表明鲢鱼肌肉中存在肌原纤维结合型蛋白酶。丝氨酸蛋白酶抑制剂(PefablocSC和利马豆胰蛋白酶抑制剂)及金属蛋白酶抑制剂EDTA有效抑制了肌球蛋白重链的分解,而其它酶类的抑制剂不产生任何作用,提示该酶为需金属离子激活的肌原纤维结合型丝氨酸蛋白酶。更多还原

【Abstract】 Myofibril-bound serine proteinase (MBSP) in the skeletal muscle of silver carp has been characterized. Myosin heavy chain (MHC) degraded markedly when silver carp myofibril was incubated at 55～60℃ as shown by SDS-PAGE. Prolonged incubation of myofibril also caused the degradation of other myofibrillar proteins such as α-actinin, actin and tropomyosin to some degree. The results suggested the existence of an endogeneous myofibril associated proteinase. Serine proteinase inhibitors (Pefabloc SC and Lima bean trypsin inhibitor) and EDTA greatly suppressed the degradation of myosin heavy chain, while inhibitors for cysteine, and asparatic proteinases did not show any effect. These effects indicated that the endogeneous proteinase was a myofibril-bound serine proteinase (MBSP) that needed metal ion(s) for activation.更多还原