Phosphorylation inhibits the activity of mu-calpain at different incubation temperatures and Ca2+ concentrations in vitro
文献类型: 外文期刊
第一作者: Du, Manting
作者: Du, Manting;Li, Xin;Li, Zheng;Li, Meng;Gao, Lingling;Zhang, Dequan;Du, Manting
作者机构:
关键词: Mutton;mu-Calpain;Phosphorylation;Temperature;Calcium
期刊名称:FOOD CHEMISTRY ( 影响因子:7.514; 五年影响因子:7.516 )
ISSN:
年卷期:
页码:
收录情况: SCI
摘要: This study aimed to investigate the effects of phosphorylation on the activity of mu-calpain and its sensitivity to temperature and Ca2+. For temperature sensitivity analysis, sarcoplasmic protein was treated with alkaline phosphatase (AP) and phosphatase inhibitor (PI) at 4, 25 and 37 degrees C. The results showed that the degradation degree of mu-calpain in the AP group was significantly higher after incubation for 12 h. For calcium sensitivity analysis, samples treated with AP and PI were incubated at 0.01, 0.05, 0.1 and 1 mM Ca2+. The results showed that the degradation rate of mu-calpain was maximum in the AP group and minimum in the PI group at 0.01, 0.05 and 0.1 mM Ca2+. The differences between the three groups reduced as concentration increased. These data demonstrate that phosphorylation plays a negative role in regulating mu-calpain activity. This study clarifies the regulatory mechanism of mu-calpain activation in vitro and/or in postmortem muscle. (C) 2017 Elsevier Ltd. All rights reserved.
分类号: TS2`TS201.2
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