Stozharov A N
Ukr Biokhim Zh (1978). 1986 Jan-Feb;58(1):5-10.
The actin-like protein with a molecular weight of 42 kDa was obtained from the preparation of freshly isolated mitochondria of the rat liver using the method of immobilized DNAse affinity chromatography. The inhibitory ability of the isolated protein with respect to pancreatic DNAse I was the same as that of muscular actin. The native structure of the mitochondria protein is confirmed by the data of spectral analysis and its ability to globular-fibrillar transformation with an increased ionic strength of the solution. The polymerization ability as well as a stimulating effect of the actin-like protein of mitochondria on the ATPase activity of myosin is much less pronounced as compared to actin of skeletal muscles.
采用固定化脱氧核糖核酸酶亲和层析法，从新鲜分离的大鼠肝脏线粒体提取物中获得了分子量为42 kDa的肌动蛋白样蛋白。分离得到的该蛋白对胰腺脱氧核糖核酸酶I的抑制能力与肌肉肌动蛋白相同。光谱分析数据以及其在溶液离子强度增加时发生球状-纤维状转变的能力证实了该线粒体蛋白的天然结构。与骨骼肌肌动蛋白相比，线粒体肌动蛋白样蛋白的聚合能力以及对肌球蛋白ATP酶活性的刺激作用要弱得多。
