MgADP与大鼠肝线粒体中H⁺-ATP酶的相互作用。

The interaction of MgADP with H+ -ATPase in rat liver mitochondria.

作者信息

Chernyak B V, Dukhovich V F

机构信息

A.N. Belozersky Laboratory of Molecular Biology and Biorganic Chemistry, Moscow State University, USSR.

出版信息

FEBS Lett. 1988 Mar 28;230(1-2):159-62. doi: 10.1016/0014-5793(88)80662-8.

DOI:10.1016/0014-5793(88)80662-8

PMID:2895017

Abstract

The activating anions are found to induce an unexpectedly high (up to 8-fold for sulphite) increase of ATPase activity in intact rat liver mitochondria. This effect is not determined by the observed changes in Km and Ki (ADP) values. The stimulation seems to be caused by dissociation of the inactive complex of ATPase with Mg.ADP. The quantity of this complex formed in the course of ATP hydrolysis is approx. 90% of the total ATPase content in intact mitochondria. The data on toluene-permeabilized mitochondria suggest that the high content of the complex is a result of the stabilizing effect of some matrix macromolecules.

摘要

已发现活化阴离子可诱导完整大鼠肝线粒体中的ATP酶活性出现意想不到的高度增加（亚硫酸盐可达8倍）。这种效应并非由观察到的Km和Ki（ADP）值的变化所决定。这种刺激似乎是由ATP酶与Mg·ADP的无活性复合物解离引起的。在ATP水解过程中形成的这种复合物的量约为完整线粒体中总ATP酶含量的90%。关于经甲苯通透处理的线粒体的数据表明，该复合物的高含量是某些基质大分子稳定作用的结果。