EFFECT OF CALPONIN ON ACTIN-ACTIVATED MYOSIN ATPASE ACTIVITY

被引：147

作者：

ABE, M

TAKAHASHI, K

HIWADA, K

机构：

[1] The Second Department of Internal Medicine, Ehime University School of Medicine, Onsen-gun

来源：

JOURNAL OF BIOCHEMISTRY | 1990年 / 108卷 / 05期

关键词：

D O I：

10.1093/oxfordjournals.jbchem.a123289

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Calponin inhibited the actin-activated myosin MgATPase activity in a dose-dependent manner without affecting the phosphorylation level of myosin light chain. This inhibition was Ca2+-independent. The decrease in enzymatic activity of myosin was correlated with binding of calponin to actin-tropomyosin filaments. Caldesmon showed a further inhibition of the calponin-induced inhibition of MgATPase activity of the thiophosphorylated myosin. Calponin-induced inhibition of the myosin MgATPase activity was reversed by the addition of calmodulin only in the presence of Ca2+. These results suggest that calponin acts as an inhibitory component of smooth muscle thin filaments. © 1990 Copyright, 1990 by the Journal of Biochemistry.

引用

页码：835 / 838

页数：4

共 43 条

[1] SIMPLIFIED COPURIFICATION OF VASCULAR SMOOTH-MUSCLE CALPONIN AND CALDESMON [J].