Calponin-like protein from mussel smooth muscle is a competitive inhibitor of actomyosin ATPase

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• 作者：V. V. Sirenko ; A. V. Dobrzhanskaya ; N. S. Shelud’ko…
• 关键词：calponin ; like protein ; mussel ; ATPase ; V max ; K ATPase ; actomyosin ; S1
• 刊名：Biochemistry (Moscow)
• 出版年：2016
• 出版时间：January 2016
• 年：2016
• 卷：81
• 期：1
• 页码：28-33
• 全文大小：226 KB
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• 作者单位：V. V. Sirenko (1)
  A. V. Dobrzhanskaya (2)
  N. S. Shelud’ko (2)
  Y. S. Borovikov (1)
  
  1. Institute of Cytology, Russian Academy of Sciences, 194064, St. Petersburg, Russia
  2. Zhirmunsky Institute of Marine Biology, Far Eastern Division, Russian Academy of Sciences, 690041, Vladivostok, Russia
  
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Biochemistry
  Bioorganic Chemistry
  Microbiology
  Biomedicine
  Russian Library of Science
  
• 出版者：MAIK Nauka/Interperiodica distributed exclusively by Springer Science+Business Media LLC.
• ISSN：1608-3040

文摘

The goal of this work was to elucidate the mechanism of inhibition of the actin-activated ATPase of myosin subfragment-1 (S1) by the calponin-like protein from mussel bivalve muscle. The calponin-like protein (Cap) is a 40-kDa actin-binding protein from the bivalve muscle of the mussel Crenomytilus grayanus. Kinetic parameters V _max and K _ATPase of actomyosin ATPase in the absence and the presence of Cap were determined to investigate the mechanism of inhibition. It was found that Cap mainly causes increase in K _ATPase value and to a lesser extent the decrease in V _max, which indicates that it is most likely a competitive inhibitor of actomyosin ATPase. Analysis of V _max and K _ATPase parameters in the presence of tropomyosin revealed that the latter is a noncompetitive inhibitor of the actomyosin ATPase. Keywords calponin-like protein mussel ATPase V _max K _ATPase actomyosin S1