Stozharov A N
Biokhimiia. 1983 Dec;48(12):2016-22.
A comparative study of the primary structure of a mitochondrial polypeptide (Mr = 42000), using a peptide mapping technique, has demonstrated its similarity to actin, especially to that isolated from smooth muscle. The actin-like protein content in liver mitochondria is 2%. The protein is readily removed from the organelles but remains tightly bound to the mitochondria after addition of the high molecular weight compound polyvinylpyrrolidone to the isolation medium. The data obtained are discussed in terms of conservative structure of the action molecule.
利用肽图技术对一种线粒体多肽（相对分子质量为42000）的一级结构进行的比较研究表明，它与肌动蛋白相似，尤其与从平滑肌中分离出的肌动蛋白相似。肝线粒体中肌动蛋白样蛋白的含量为2%。该蛋白很容易从细胞器中去除，但在分离介质中加入高分子量化合物聚乙烯吡咯烷酮后，它仍紧密结合在线粒体上。根据肌动蛋白分子的保守结构对所获得的数据进行了讨论。
