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首页> 外文会议>International Symposium on the Efficient Application and Preservation of Marine Biological Resourecs; 20041029-1102; Qingdao(CN) >Degradation of myofibrillar proteins by a myofibril-bound serine proteinase in the skeletal muscle of crucian carp
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Degradation of myofibrillar proteins by a myofibril-bound serine proteinase in the skeletal muscle of crucian carp

机译：my鱼骨骼肌中肌原纤维结合的丝氨酸蛋白酶降解肌原纤维蛋白

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摘要

Myofibril-bound serine proteinase (MBSP) in the skeletal muscle of crucian carp was identified. Hydrolysis of myofibrillar proteins by the endogenous MBSP was studied. Myosin heavy chain (MHC) degraded markedly when crucian carp myoftbrii was incubated at around 55℃ as shown by SDS-PAGE. Prolonged incubation of myofibril at 55℃ also caused the obvious degradation of tropomyosin, while the decomposition of other myofibrillar proteins such as a-actinin and actin was slight as detected by Western blotting. The results suggest the existence of an endogenous myofibril associated proteinase in crucian carp myofibril, which efficiently cleaves MHC and tropomyosin. Serine proteinase inhibitors (Lima bean trypsin inhibitor, PMSF and benzamidine) greatly suppressed the degradation of MHC caused by the enzyme, while inhibitors for cysteine, metallo, and asparatic proteinases only partially or completely did not show any inhibitory effect, indicating that the endogenous proteinase is a serine proteinase. Substrate specificity analysis using partial purified crucian carp MBSP suggested that the enzyme is a trypsin-like serine proteinase.
机译：在cru鱼的骨骼肌中发现了肌原纤维结合的丝氨酸蛋白酶（MBSP）。研究了内源性MBSP对肌原纤维蛋白的水解作用。如SDS-PAGE所示，when鱼肌纤维在55℃左右孵育时，肌球蛋白重链（MHC）明显降解。肌原纤维在55℃下长时间孵育也会引起原肌球蛋白的明显降解，而其他肌原纤维蛋白（如α-肌动蛋白和肌动蛋白）的分解通过Western blotting检测则很小。结果表明cru鱼肌原纤维中存在内源性肌原纤维相关蛋白酶，可有效裂解MHC和原肌球蛋白。丝氨酸蛋白酶抑制剂（利马豆胰蛋白酶抑制剂，PMSF和苯甲idine）极大地抑制了该酶引起的MHC降解，而半胱氨酸，金属和天冬氨酸蛋白酶的抑制剂仅部分或完全没有抑制作用，表明内源蛋白酶是丝氨酸蛋白酶。使用部分纯化的cru鱼MBSP的底物特异性分析表明该酶是一种胰蛋白酶样丝氨酸蛋白酶。

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