Volodina T V, Koloskova E E, Shishkin S S, Kozel'tsev V L
Vopr Med Khim. 1987 Jul-Aug;33(4):25-8.
About 50 protein fractions with molecular mass 15-158 kDa were detected in purified mitochondria isolated from rat liver homogenate after two-dimensional electrophoresis performed as described by O'Farrell. Individual spots, corresponding to proteins of inner mitochondrial membrane, disappeared from electrophoregrams as a result of incubation of the isolated mitochondria at 37 degrees and pH 7.5. Degradation of these proteins was augmented if ATP was added into incubation mixtures. Intrinsic proteolytic activity occurred in rat liver mitochondria as shown by these and previously obtained data.
按照奥法雷尔所述方法进行二维电泳后，从大鼠肝脏匀浆中分离出的纯化线粒体中检测到约50种分子量在15 - 158 kDa之间的蛋白质组分。对应线粒体内膜蛋白质的各个斑点，由于分离出的线粒体在37摄氏度和pH值7.5条件下孵育，从电泳图谱上消失了。如果在孵育混合物中添加ATP，这些蛋白质的降解会加剧。这些数据以及之前获得的数据表明，大鼠肝脏线粒体中存在内在的蛋白水解活性。
