Calponin-like protein from mussel smooth muscle is a competitive inhibitor of actomyosin ATPase
- Authors: Sirenko V.V.1, Dobrzhanskaya A.V.2, Shelud’ko N.S.2, Borovikov Y.S.1
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Affiliations:
- Institute of Cytology, Russian Academy of Sciences
- Zhirmunsky Institute of Marine Biology
- Issue: Vol 81, No 1 (2016)
- Pages: 28-33
- Section: Article
- URL: https://journals.rcsi.science/0006-2979/article/view/150758
- DOI: https://doi.org/10.1134/S000629791601003X
- ID: 150758
Cite item
Abstract
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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About the authors
V. V. Sirenko
Institute of Cytology, Russian Academy of Sciences
Email: boroviko@mail.cytspb.rssi.ru
Russian Federation, St. Petersburg, 194064
A. V. Dobrzhanskaya
Zhirmunsky Institute of Marine Biology
Email: boroviko@mail.cytspb.rssi.ru
Russian Federation, Vladivostok, 690041
N. S. Shelud’ko
Zhirmunsky Institute of Marine Biology
Author for correspondence.
Email: sheludko@stl.ru
Russian Federation, Vladivostok, 690041
Y. S. Borovikov
Institute of Cytology, Russian Academy of Sciences
Author for correspondence.
Email: boroviko@mail.cytspb.rssi.ru
Russian Federation, St. Petersburg, 194064