Phosphorylation prevents in vitro myofibrillar proteins degradation by μ-calpain
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- 作者：Zheng Lia ; 1 ; lizheng1986114@163.com" class="auth_mail" title="E-mail the corresponding author ; Xin Lia ; Xing Gaoa ; Qingwu W. Shenb ; Manting Dua ; Dequan Zhanga ; dequan_zhang0118@126.com" class="auth_mail" title="E-mail the corresponding author
- 关键词：PKA ; protein kinase A ; AP ; alkaline phosphatase ; LD ; Longissimus dorsi ; EGTA ; ethylene glycol tetraacetic acid ; DTT ; dithiothreitol ; BCA ; bicinchoninic acid ; ATP ; adenosine triphosphate ; SDS-PAGE ; sodium dodecyl sulfate-polyacrylamide gel electrophoresis ; PVDF ; polyvinylidene fluoride ; BSA ; bull serum albumin ; TBST ; tris buffered saline Tween 20 ; HRP ; horse radish peroxidase ; ECL ; electrochemiluminescence ; TnT ; troponin T ; MHC ; myosin heavy chain
- 刊名：Food Chemistry
- 出版年：2017
- 出版时间：1 March 2017
- 年：2017
- 卷：218
- 期：Complete
- 页码：455-462
- 全文大小：1157 K
文摘
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Myofibrillar proteins treated by protein kinase A and alkaline phosphatase were degraded by μ-calpain.
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Degradation of myosin heavy chain, actin, desmin and troponin T was analysed.
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Phosphorylation prevents myofibrillar proteins degradation by μ-calpain.
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Dephosphorylation enhances myofibrillar proteins degradation by μ-calpain.