STIMULATORY EFFECT OF CALPONIN ON MYOSIN ATPASE ACTIVITY

被引:36
作者
LIN, Y [1 ]
YE, LH [1 ]
ISHIKAWA, R [1 ]
FUJITA, K [1 ]
KOHAMA, K [1 ]
机构
[1] GUNMA UNIV,SCH MED,DEPT PHARMACOL,MAEBASHI,GUNMA 371,JAPAN
关键词
D O I
10.1093/oxfordjournals.jbchem.a124096
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, a calmodulin-binding protein of smooth muscle that inhibits the actin myosin interaction by binding to actin, was shown to bind to myosin and to stimulate the ATPase activity of myosin to some extent. Actin abolished this myosin-linked, stimulatory effect of calponin. Ca2+-calmodulin affected neither the myosin-binding activity nor the stimulatory effect of calponin. We further presented a few data which suggest that calponin may exert regulatory activity toward myosin in quite a different way from caldesmon, another smooth muscle protein that binds to myosin, actin, and calmodulin.
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收藏
页码:643 / 645
页数:3
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