The isolation of dicyclohexylcarbodi-imide-binding proteins from mitochondrial membranes.
The isolation of dicyclohexylcarbodi-imide-binding proteins from mitochondrial membranes.
复制标题
从线粒体膜中分离二环己基碳二亚胺结合蛋白。
作者：
K. J. Cattell;I. G. Knight;C. Lindop;R. Beechey
DCCD* 是氧化磷酸化的有效抑制剂。有人认为，它的作用位点可能是ATP合成的中间体，与之形成共价键（Beechey，Roberton，霍洛威和Knight，1967）。因此，需要分离和表征DCCD与之相互作用的微扰子中的组分。Knight、霍洛威、Roberton和Beechey（1968）已经表明，当线粒体制备物中含有两种蛋白脂质组分时，[14 C] DCCD处理的线粒体或亚线粒体颗粒中的放射性被回收。
DCCD* is a potent inhibitor of oxidative phosphorylation. It has been suggested that its site of action may be an intermediate of ATP synthesis with which it forms a covalent bond (Beechey, Roberton, Holloway & Knight, 1967). Therefore it is desirable to isolate and characterize the component(s) in the mitochondrion with which DCCD interacts. Knight, Holloway, Roberton & Beechey (1968) have shown that the radioactivity in [14C]DCCD-treated mitochondria or submitochondrial particles was recovered with two proteolipid fractions when the mitochondrial preparations