Azzi A, Bill K, Broger C
Proc Natl Acad Sci U S A. 1982 Apr;79(8):2447-50. doi: 10.1073/pnas.79.8.2447.
An efficient affinity chromatography procedure for the isolation of mitochondrial cytochrome c oxidase and reductase is described. Saccharomyces cerevisiae cytochrome c was used as a ligand, bound to a thiol-Sepharose 4B gel through cysteine-107. In this way, the site of interaction of cytochrome c with cytochrome oxidase and reductase remained unmodified and available for binding to a number of partner enzymes. The procedure is adequate for the purification of all those proteins having in common the property of binding with high affinity to cytochrome c--e.g., cytochrome c oxidase, reductase, and peroxidase, sulfite oxidase, and reaction centers of photosynthetic bacteria.
本文描述了一种用于分离线粒体细胞色素c氧化酶和还原酶的高效亲和色谱方法。酿酒酵母细胞色素c用作配体，通过半胱氨酸-107与硫醇-琼脂糖4B凝胶结合。通过这种方式，细胞色素c与细胞色素氧化酶和还原酶的相互作用位点未被修饰，可用于与多种伴侣酶结合。该方法适用于纯化所有具有与细胞色素c高亲和力结合特性的蛋白质，例如细胞色素c氧化酶、还原酶、过氧化物酶、亚硫酸盐氧化酶以及光合细菌的反应中心。
