In vitro proteolysis of myofibrillar and sarcoplasmic proteins of white muscle of sea bass (Dicentrarchus labrax L.):: effects of cathepsins B, D and L
In vitro proteolysis of myofibrillar and sarcoplasmic proteins of white muscle of sea bass (Dicentrarchus labrax L.):: effects of cathepsins B, D and L
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DOI：
10.1016/s0308-8146(02)00481-8
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发表时间：
2003-06-01
期刊：
影响因子：
8.8
通讯作者：
Fleurence, J
中科院分区：
文献类型：
--
作者：
Ladrat, C;Verrez-Bagnis, V;Fleurence, J
本研究的目的是获得更多的信息，蛋白质水解机制和解体的鱼肌原纤维导致的损失的肉品质。研究了组织蛋白酶在体外降解鱼肌肉中肌原纤维和肌浆蛋白的能力，以解释它们在死后软化中的作用。这导致了酶的底物的鉴定。组织蛋白酶降解肌球蛋白重链和α-辅肌动蛋白。原肌球蛋白和肌动蛋白只对组织蛋白酶L的作用敏感。肌钙蛋白T（假定为32 kDa组分）仅对组织蛋白酶D的作用具有抗性。结蛋白被组织蛋白酶B和L降解。还观察到一些其他肌原纤维或胞质蛋白的轻微变化（肌酸激酶和其他未鉴定的蛋白）。当与在储存的死后肌肉中观察到的蛋白质修饰相比时，这些结果表明组织蛋白酶D（如果位置在细胞质中并且如果死后肌肉中满足活性的pH条件）可能参与死后肌原纤维降解机制。(C)2002爱思唯尔科技有限公司版权所有。
The purpose of this study was to obtain additional information regarding proteolysis mechanisms and disorganization of fish myofibrils resulting in a loss of flesh quality. The ability of cathepsins to degrade in vitro myofibrillar and sarcoplasmic proteins from fish muscle was investigated in order to explain their role in post mortem softening. This led to the identification of substrates of the enzymes. Cathepsins degraded myosin heavy chain and a-actinin. Tropomyosin and actin were only susceptible to the action of cathepsin L. Troponin T (assumed 32 kDa component) was resistant only to the action of cathepsin D. Desmin was degraded by cathepsins B and L. Slight changes of some other myofibrillar or cytosolic proteins were also observed (creatine kinase and other unidentified proteins). When compared with protein modifications observed in stored post mortem muscle, these results suggest that cathepsin D (if location is in the cytosol and if pH conditions for activity are met in post mortem muscle) could be involved in a post mortem myofibrillar degradation mechanism. (C) 2002 Elsevier Science Ltd. All rights reserved.