IS PHOSPHORYLATION THE MAIN PHYSIOLOGICAL ACTION OF MYOSIN LIGHT-CHAIN KINASE

被引:3
作者
EBASHI, S [1 ]
KUWAYAMA, H [1 ]
机构
[1] OBIHIRO UNIV AGR & VET MED,CHEM LAB,OBIHIRO,HOKKAIDO,JAPAN
关键词
MYOSIN LIGHT CHAIN KINASE; PHOSPHORYLATION OF MYOSIN LIGHT CHAIN; LEIOTONIN; WORTMANNIN; BERYLLIUM SULFATE;
D O I
10.1139/y94-198
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
The 155-kDa component of bovine stomach, which exhibits a strong actomyosin (AM) activating activity and a relatively weak myosin light chain kinase (MLCK) activity, has a strong affinity for the actin filament and the actin-binding site is confined to an 80 amino acid residue on its N-terminal side. This affinity may play a crucial role in AM activation. Some reagents preferentially abolish either the AM-activating effect or MLCK activity. In conclusion, MLCK of the 155-kDa component does not play a fundamental role in activating the AM system as far as the in vitro system is concerned. The possible mechanism of AM activation by the component is discussed.
引用
收藏
页码:1377 / 1379
页数:3
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