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[细菌膜蛋白。通过电聚焦法纯化NADH脱氢酶]

[Proteins of bacterial membranes. Purification of NADH-dehydrogenase by electrofocusing].

作者信息

Zhukova I G, Shaposhnikov G L, Ostrovskii D N

出版信息

Biokhimiia. 1976 Oct;41(10):1840-5.

PMID:1030633
Abstract

A highly purified preparation of NADH dehydrogenase was isolated from bacteria M. lysodeikticus membranes. The purification procedure involved extraction of the enzyme complex from isolated membranes by EDTA, solubilization of the complex by non-ionogenic detergent (1% Triton X-100), chromatography on DEAE-cellulose and electrofocussing in the pH gradient 4-6. The isoelectric point of the preparation is at 4.5; its main component is a protein with m.w. of about 76.000.

摘要

从溶壁微球菌(Micrococcus lysodeikticus)细胞膜中分离出了一种高度纯化的NADH脱氢酶制剂。纯化过程包括用EDTA从分离的细胞膜中提取酶复合物,用非离子型去污剂(1% Triton X-100)溶解该复合物,在DEAE-纤维素上进行色谱分离,并在pH 4-6梯度中进行电聚焦。该制剂的等电点为4.5;其主要成分是一种分子量约为76000的蛋白质。

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