Ozerniuk N D, Kotomin A V
Biokhimiia. 1978 Jan;43(1):67-71.
The in vitro transport into mitochondria of proteins synthesized in the cytoplasm was studied. The system, in which the microsomes synthesize protein in the presence of mitochondria directly during the experiment proved to be the most efficient one. The microsomal fraction significantly stimulated the incorporation of 14C-valine into the isolated mitochondria proteins. The effects of EDTA treatment of the mitochondrial fraction, the dependence of protein synthesis stimulation on the ratio of mitochondria and microsomal proteins and the kinetic pattern of the reaction suggest that the stimulation of the labelled precursor incorporation into mitochondrial proteins is not probably due to the labelled microsomes adsorption on the mitochondria.
研究了细胞质中合成的蛋白质在线粒体内的体外转运。实验证明，在实验过程中微粒体直接在线粒体存在的情况下合成蛋白质的系统是最有效的。微粒体部分显著刺激了14C-缬氨酸掺入分离的线粒体蛋白质中。线粒体部分经EDTA处理的效果、蛋白质合成刺激对线粒体和微粒体蛋白质比例的依赖性以及反应的动力学模式表明，标记前体掺入线粒体蛋白质的刺激作用可能不是由于标记的微粒体吸附在线粒体上。
