Dubiel W, Henke W, Miura Y, Holzhütter H G, Gerber G
Institute of Biochemistry, Humboldt University, Berlin, GDR.
Biochem Int. 1987 Jul;15(1):45-54.
A novel ATPase is postulated for isolated mitochondria and mitoblasts of rat liver. The enzyme is active in the presence of oligomycin and carboxyatractyloside. It can be distinguished from other well-known mitochondrial and non-mitochondrial ATPases by its insensitivity to common ATPase inhibitors and effectors and by digitonin treatment. The ATPase is localized on the outer side of the inner mitochondrial membrane. It is activated by Mg2+ in the alkaline pH range and exhibits a biphasic kinetics. The novel external ATPase of rat liver mitochondria possesses similar properties with respect to ATP-dependent protease.
一种新的ATP酶被假定存在于大鼠肝脏的分离线粒体和线粒体芽中。该酶在寡霉素和羧基苍术苷存在的情况下具有活性。它可以通过对常见ATP酶抑制剂和效应物不敏感以及经洋地黄皂苷处理与其他著名的线粒体和非线粒体ATP酶区分开来。该ATP酶定位于线粒体内膜外侧。它在碱性pH范围内被Mg2+激活,并呈现双相动力学。大鼠肝脏线粒体新的外部ATP酶在依赖ATP的蛋白酶方面具有相似特性。