大鼠肝脏线粒体在体外对纯化的天冬氨酸氨基转移酶的选择通透性。
Selective permeability of rat liver mitochondria to purified aspartate aminotransferases in vitro.
作者信息
Marra E, Doonan S, Saccone C, Quagliariello E
出版信息
Biochem J. 1977 Jun 15;164(3):685-91. doi: 10.1042/bj1640685.
Abstract
- A method was devised to allow determination of intramitochondrial aspartate amino-transferase activity in suspensions of intact mitochondria. 2. Addition of purified rat liver mitochondrial aspartate aminotransferase to suspensions of rat liver mitochondria caused an apparent increase in the intramitochondrial enzyme activity. No increase was observed when the mitochondria were preincubated with the purified cytoplasmic isoenzyme. 3. These results suggest that mitochondrial aspartate aminotransferase, but not the cytoplasmic isoenzyme, is able to pass from solution into the matrix of intact rat liver mitochondria in vitro. 4. This system may provide a model for studies of the little-understood processes by which cytoplasmically synthesized components are incorporated into mitochondria in vivo.
摘要
- 设计了一种方法，用于测定完整线粒体悬浮液中的线粒体内天冬氨酸氨基转移酶活性。2. 向大鼠肝线粒体悬浮液中添加纯化的大鼠肝线粒体天冬氨酸氨基转移酶，导致线粒体内酶活性明显增加。当线粒体与纯化的细胞质同工酶预孵育时，未观察到活性增加。3. 这些结果表明，在线体外，线粒体天冬氨酸氨基转移酶而非细胞质同工酶能够从溶液进入完整大鼠肝线粒体的基质。4. 该系统可为研究体内细胞质合成成分如何整合到线粒体这一了解甚少的过程提供模型。
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