Maruyama K, Kunitomo S, Kimura S, Ohashi K
J Biochem. 1977 Jan;81(1):243-7. doi: 10.1093/oxfordjournals.jbchem.a131441.
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.
在低离子强度下,I蛋白可使肌动球蛋白的镁激活ATP酶[EC 3.6.1.3]活性降低约50%。同时,超沉淀的起始被延迟。发现I蛋白与肌球蛋白结合,但不与F-肌动蛋白结合。I蛋白的抑制作用仅在肌钙蛋白-原肌球蛋白-肌动蛋白-肌球蛋白系统中不存在钙离子时发生。添加钙离子可消除该效应。因此,I蛋白很可能在肌肉松弛状态下防止ATP的不必要水解。