来自山羊支原体的含黄素腺嘌呤二核苷酸（FAD）的NADH氧化酶的纯化及性质

Purification and properties of an FAD-containing NADH oxidase from Mycoplasma capricolum.

作者信息

Klömkes M, Altdorf R, Ohlenbusch H D

出版信息

Biol Chem Hoppe Seyler. 1985 Oct;366(10):963-9. doi: 10.1515/bchm3.1985.366.2.963.

DOI:10.1515/bchm3.1985.366.2.963

Abstract

From the prokaryotic microorganism Mycoplasma capricolum an FAD-containing NADH oxidase has been purified by preparative FPLC to homogeneity, as judged by polyacrylamide gel electrophoresis. The apparent molecular mass of the enzyme was found to be 72.5 kDa, with an isoelectric point of 5.2, and no detectable subunits. No iron, copper, manganese or molybdenium could be detected. On the basis of a minimum molecular mass of 72.5 kDa a ratio of FAD/protein of 1:1 could be derived. Its amino-acid composition, the light absorption and the fluorescence spectra are presented.

摘要

从原核微生物山羊支原体中，通过制备型快速蛋白质液相色谱法纯化得到了一种含黄素腺嘌呤二核苷酸（FAD）的烟酰胺腺嘌呤二核苷酸（NADH）氧化酶，经聚丙烯酰胺凝胶电泳判断，该酶已达到同质。发现该酶的表观分子量为72.5 kDa，等电点为5.2，且未检测到亚基。未检测到铁、铜、锰或钼。基于72.5 kDa的最小分子量，可以得出FAD/蛋白质的比例为1:1。文中给出了其氨基酸组成、光吸收和荧光光谱。