酵母线粒体中细胞色素b复合物和细胞色素氧化酶的分离及部分特性分析

Isolation and partial charcterization of a cytochrome b complex and cytochrome oxidase from yeast mitochondria.

作者信息

Marjanen L A

出版信息

Prep Biochem. 1976;6(2-3):153-75. doi: 10.1080/00327487608061610.

Abstract

A cytochrome b complex and cytochrome oxidase have been purified 14- and 20-fold respectively from yeast submitochondrial particles by a simple procedure involving their spontaneous precipitation from a deoxycholate extract. The recovery of both proteins was almost quantitative. The specific heme contents were 11 and 8 nmoles/mg protein for the cytochrome b complex and cytochrome oxidase respectively and both were spectrally pure. Sodium dodecyl sulfate gel electrophoresis resolved the cytochrome b complex into seven distinct subunits with molecular weights 42,000, 33,000, 27,500, 23,000, 15,500, 13,000 and 10,500. Cytochrome oxidase contained five bands with molecular weights 42,000, 26,500, 21,000, 14,000 and 10,500.

摘要

通过一种简单的方法，即从脱氧胆酸盐提取物中自发沉淀，分别从酵母亚线粒体颗粒中纯化出细胞色素b复合物和细胞色素氧化酶，纯化倍数分别为14倍和20倍。两种蛋白质的回收率几乎是定量的。细胞色素b复合物和细胞色素氧化酶的特定血红素含量分别为11和8纳摩尔/毫克蛋白质，且两者在光谱上均为纯品。十二烷基硫酸钠凝胶电泳将细胞色素b复合物分解为七个不同的亚基，分子量分别为42,000、33,000、27,500、23,000、15,500、13,000和10,500。细胞色素氧化酶含有五条带，分子量分别为42,000、26,500、21,000、14,000和10,500。