Volodina T V, Kozel'tsev V L
Biokhimiia. 1978 Oct;43(10):1816-22.
Highly purified mitochondria and lysosomes are isolated from rat liver homogenate. pH optimum of proteolytic activity with respect to proteins of own structures and to mitochondrial structural protein is investigated. The purification of mitochondria from lysosomes is found to be accompanied by the change of proteolytic activity pH optimum from 5.0 to 6.0 in coarse and purified mitochondria respectively. Comparative study of structural protein hydrolysis products with enzyme preparations from purified mitochondria and lysosomes has revealed differences in the spectrum of the reaction products. The data obtained suggest a presence of a proteolytic enzyme in rat liver mitochondria.
从大鼠肝脏匀浆中分离出高度纯化的线粒体和溶酶体。研究了针对自身结构蛋白和线粒体结构蛋白的蛋白水解活性的最适pH值。发现从溶酶体中纯化线粒体时，粗线粒体和纯化线粒体中蛋白水解活性的最适pH值分别从5.0变为6.0。对纯化的线粒体和溶酶体中的酶制剂水解结构蛋白产物的比较研究揭示了反应产物谱的差异。所获得的数据表明大鼠肝脏线粒体中存在一种蛋白水解酶。
