Dephosphorylation of myosin regulatory light chain modulates actin-myosin interaction adverse to meat tenderness

文献类型： 外文期刊

第一作者： Gao, Xing

作者： Gao, Xing;Li, Xin;Li, Zheng;Du, Manting;Zhang, Dequan;Gao, Xing

作者机构：

关键词： Actomyosin dissociation;ATPase activity;dephosphorylation;myosin regulation light chain

期刊名称：INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY （ 影响因子：3.713； 五年影响因子：3.408 ）

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收录情况： SCI

摘要： The objective of this study was to investigate the relationship between the dephosphorylation of myosin regulatory light chain and actin-myosin interaction after muscle homogenate was treated with alkaline phosphatase and phosphatase inhibitor. The myosin regulatory light chain was significantly dephosphorylated by alkaline phosphatase after incubation. Among different groups, dephosphorylated myosin regulatory light chain to a much greater extent leads to a lower actomyosin dissociation degree, thereby raising the actomyosin ATPase activity, whereas it exhibits a higher actomyosin dissociation degree and a lower actomyosin ATPase activity when the myosin regulatory light chain was in a low dephosphorylated state. The data suggest that the dephosphorylation of myosin regulatory light chain modulates actomyosin dissociation (the number of myosin interact with actin) negatively and has a positive influence on actomyosin ATPase activity (the interacting force between myosin and actin).

分类号： TS2

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