I-protein, a new regulatory protein from vertebrate skeletal muscle. III. Function.
作者信息
Maruyama K, Kunitomo S, Kimura S, Ohashi K
出版信息
J Biochem. 1977 Jan;81(1):243-7. doi: 10.1093/oxfordjournals.jbchem.a131441.
Abstract
I-protein inhibited theMg-activated ATPase [EC 3.6.1.3] activity of actinomyosin by approximately 50% at low ionic strength. Concomitantly, the onset of superprecipitation was retarded. I-protein was found to bind to myosin, but not to F-actin. The inhibitory action of I-protein occurred only in the absence of Ca ions in the troponintropomyosin-actin myosin system. Addition of Ca ions abolished the effect. Thus, it is very likely that I-protein prevents unnecessary hydrolysis of ATP in the relaxed state of muscle.
摘要
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