肌原纤维
结蛋白
卡尔帕因
肌节
化学
肌钙蛋白
肌动蛋白
肌钙蛋白T
蛋白质降解
肌球蛋白
蛋白质水解
肌钙蛋白I
提丁
生物化学
钙蛋白酶抑制剂
细胞生物学
内科学
酶
心肌细胞
生物
医学
免疫组织化学
波形蛋白
心肌梗塞
作者
Zheng Li,Xin Li,Xing Gao,Ming Du,Dequan Zhang
摘要
Abstract BACKGROUND Tenderness is considered to be one of the most important attributes of meat quality. Myofibrillar protein degradation contributes to meat tenderization during postmortem ageing. In this process, calpain is the primary enzyme catalyzing the proteolysis. To further understand the action of calpain in meat tenderization, a μ ‐calpain inhibitor, MDL ‐28170, was used and its effects on sarcomere structure and myofibrillar protein degradation were determined. RESULTS The results of the present study showed that inhibition of μ ‐calpain significantly reduced muscle myofibrillar fragmentation compared to the group without μ ‐calpain inhibitor. Meanwhile, the sarcomere structure of the μ ‐calpain inhibited muscle was only slightly broken and largely remained integral 48 h postmortem. Myosin heavy chain, actin, desmin, troponin T and troponin I were identified to be substrates of μ ‐calpain by liquid chromatography‐tandem mass spectrocopy and western blotting, and were detected with a higher degradation degree in the control group compared to the μ ‐calpain inhibition group. CONCLUSION Comparatively, myosin heavy chain and actin were found to be less sensitive to μ ‐calpain compared to desmin, troponin T and troponin I. These findings provide a better understanding of the contribution of μ ‐calpain to the myofibril structure and myofibrillar protein degradation of ovine muscle. © 2016 Society of Chemical Industry
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