Myosin Light Chain Kinase from Vascular Smooth Muscle Inhibits the ATP-Dependent Interaction between Actin and Myosin by Binding to Actin.
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概要
- 論文の詳細を見る
Myosin light chain kinase (MLCK) was prepared from smooth muscle of bovine aorta. MLCK inhibited the ATP-dependent movement of actin filaments on a glass surface coated with smooth muscle myosin that had been phosphorylated. The inhibitory effect was abolished by calmodulin in the presence of Ca2+ (Ca-CaM). The abolition was also observed when the concentration of actin filaments was increased. The inhibitory effect and its abolition were related to the actin-binding activity of MLCK, that is antagonized by Ca-CaM.
- 社団法人 日本生化学会の論文
著者
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Sato Manabu
Department of Cardiology, Kouseikai Hospital
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Kohama Kazuhiro
Department Of Molecular And Cellular Pharmacology Faculty Of Medicine Gunma University Graduate Scho
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YE Li-Hong
Department of Biochemistry, College of Life Sciences, Nankai University
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