鱼类肌球蛋白亚片段-1的结构稳定性
Structural stability of fish myosin subfragment-1.
作者信息
Hamai M, Konno K
机构信息
Department of Food Science, Faculty of Fisheries, Hokkaido University, Japan.
出版信息
Comp Biochem Physiol B. 1990;95(2):255-9. doi: 10.1016/0305-0491(90)90073-3.
PMID:2328565
Abstract
- Tryptic cleavage of fish myosin subfragment-1 (S-1) revealed its similar substructure of heavy chain to that of rabbit S-1. 2. The structural stability of fish S-1 was studied by thermal denaturation method, and a rapid polymerization of inactivated fish S-1, detected by turbidity increase, was characteristic. 3. The light-chain release and tryptic susceptibility increase upon heating were significant with fish S-1.
摘要
- 用胰蛋白酶裂解鱼肌球蛋白亚片段-1（S-1），发现其重链的亚结构与兔S-1相似。2. 采用热变性方法研究了鱼S-1的结构稳定性，通过浊度增加检测到失活的鱼S-1会快速聚合，这是其特征。3. 加热时，鱼S-1的轻链释放和对胰蛋白酶的敏感性增加显著。
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