Phosphorylation prevents in vitro myofibrillar proteins degradation by μ-calpain

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Phosphorylation prevents in vitro myofibrillar proteins degradation by μ-calpain

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作者：Zheng Li^a ; ¹ ; ^{lizheng1986114@163.com" class="auth_mail" title="E-mail the corresponding author} ; Xin Li^a ; Xing Gao^a ; Qingwu W. Shen^b ; Manting Du^a ; Dequan Zhang^a ; ^{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

•: Myofibrillar proteins treated by protein kinase A and alkaline phosphatase were degraded by μ-calpain.
•: Degradation of myosin heavy chain, actin, desmin and troponin T was analysed.
•: Phosphorylation prevents myofibrillar proteins degradation by μ-calpain.
•: Dephosphorylation enhances myofibrillar proteins degradation by μ-calpain.

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