Calponin-like protein from mussel smooth muscle is a competitive inhibitor of actomyosin ATPase
- 作者: Sirenko V.1, Dobrzhanskaya A.2, Shelud’ko N.2, Borovikov Y.1
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隶属关系:
- Institute of Cytology, Russian Academy of Sciences
- Zhirmunsky Institute of Marine Biology
- 期: 卷 81, 编号 1 (2016)
- 页面: 28-33
- 栏目: Article
- URL: https://journals.rcsi.science/0006-2979/article/view/150758
- DOI: https://doi.org/10.1134/S000629791601003X
- ID: 150758
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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 Vmax and KATPase 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 KATPase value and to a lesser extent the decrease in Vmax, which indicates that it is most likely a competitive inhibitor of actomyosin ATPase. Analysis of Vmax and KATPase parameters in the presence of tropomyosin revealed that the latter is a noncompetitive inhibitor of the actomyosin ATPase.
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作者简介
V. Sirenko
Institute of Cytology, Russian Academy of Sciences
Email: boroviko@mail.cytspb.rssi.ru
俄罗斯联邦, St. Petersburg, 194064
A. Dobrzhanskaya
Zhirmunsky Institute of Marine Biology
Email: boroviko@mail.cytspb.rssi.ru
俄罗斯联邦, Vladivostok, 690041
N. Shelud’ko
Zhirmunsky Institute of Marine Biology
编辑信件的主要联系方式.
Email: sheludko@stl.ru
俄罗斯联邦, Vladivostok, 690041
Y. Borovikov
Institute of Cytology, Russian Academy of Sciences
编辑信件的主要联系方式.
Email: boroviko@mail.cytspb.rssi.ru
俄罗斯联邦, St. Petersburg, 194064