鸡肝线粒体苹果酸脱氢酶的纯化。少量胞质同工酶的存在。

Purification of malate dehydrogenase from chicken liver mitochondria. Existence of a small quantity of cytosolic isoenzyme.

Gelpí J L, Domènech C, Mazo A, Cortés A, Bozal J

Departament de Bioquímica i Fisiologia, Facultat de Química, Universitat de Barcelona, Spain.

Int J Biochem. 1988;20(9):989-96. doi: 10.1016/0020-711x(88)90186-3.

Abstract

A new purification method for chicken liver mitochondrial malate dehydrogenase is described. The application of affinity chromatography through 5'AMP-Sepharose and Blue-Sepharose permits to obtain homogeneous preparations, with good yields (47%), in a short time (48 hr). 2. The 5'AMP-Sepharose chromatography reveals the presence of two malate dehydrogenase species in the mitochondrial extracts. 3. A comparative study of these forms point out the cytosolic nature of the minority form and suggests that its presence could be due to a slight interaction of the cytosolic malate dehydrogenase with mitochondrial membranes.

摘要

本文描述了一种鸡肝线粒体苹果酸脱氢酶的新纯化方法。通过5'-腺苷酸-琼脂糖亲和层析和蓝色琼脂糖亲和层析，能够在短时间内（48小时）以较高产率（47%）获得均一的制剂。2. 5'-腺苷酸-琼脂糖层析显示线粒体提取物中存在两种苹果酸脱氢酶。3. 对这些形式的比较研究指出了少数形式的胞质性质，并表明其存在可能是由于胞质苹果酸脱氢酶与线粒体膜之间的轻微相互作用。