Is phosphorylation the main physiological action of myosin light chain kinase?
Is phosphorylation the main physiological action of myosin light chain kinase?
复制标题
磷酸化是肌球蛋白轻链激酶的主要生理作用吗?
DOI:
10.1139/y94-198
复制
发表时间:
1994
影响因子:
2.1
通讯作者:
H. Kuwayama
中科院分区:
文献类型:
--
作者:
S. Ebashi;H. Kuwayama
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.
影响因子:
20.1
作者:
DeLanerolle,P;Strauss,JD;Felsen,R;Doerman,GE;Paul,RJ
通讯作者:
Paul,RJ