Effect of Cardiac Myosin-Binding Protein C on Tropomyosin Regulation of Actin—Myosin Interaction Using In Vitro Motility Assay
- 作者: Shchepkin D.1, Kopylova G.1, Nikitina L.1
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隶属关系:
- Institute of Immunology and Physiology, Ural Division of the Russian Academy of Sciences
- 期: 卷 162, 编号 1 (2016)
- 页面: 45-47
- 栏目: Article
- URL: https://journals.rcsi.science/0007-4888/article/view/237890
- DOI: https://doi.org/10.1007/s10517-016-3541-9
- ID: 237890
如何引用文章
详细
We studied the modulating role of cardiac myosin-binding protein C (cMyBP-C) in tropomyosin regulation of the actin—myosin interaction. The effect of cMyBP-C on the velocity of actin-tropomyosin filament sliding over cardiac and slow skeletal myosins was evaluated using in vitro motility assay. The effect of cMyBP-C on the actin-tropomyosin filaments sliding depended on the type of myosin. The regulatory effect of cMyBP-C differs for cardiac and slow skeletal myosin because of the presence of specific essential light chain (LC1sa) in slow skeletal myosin isoform.
作者简介
D. Shchepkin
Institute of Immunology and Physiology, Ural Division of the Russian Academy of Sciences
Email: l.nikitina@iip.uran.ru
俄罗斯联邦, Ekaterinburg
G. Kopylova
Institute of Immunology and Physiology, Ural Division of the Russian Academy of Sciences
Email: l.nikitina@iip.uran.ru
俄罗斯联邦, Ekaterinburg
L. Nikitina
Institute of Immunology and Physiology, Ural Division of the Russian Academy of Sciences
编辑信件的主要联系方式.
Email: l.nikitina@iip.uran.ru
俄罗斯联邦, Ekaterinburg
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