Lipid and subunit III depleted cytochrome c oxidase purified by horse cytochrome c affinity chromatography in lauryl maltoside.
Lipid and subunit III depleted cytochrome c oxidase purified by horse cytochrome c affinity chromatography in lauryl maltoside.
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通过月桂基麦芽糖苷中的马细胞色素 c 亲和层析纯化脂质和亚基 III 耗尽的细胞色素 c 氧化酶。
DOI：
10.1021/bi00282a022
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发表时间：
1983
期刊：
影响因子：
2.9
通讯作者：
Ferguson-Miller,S
中科院分区：
文献类型：
--
作者：
Thompson,DA;Ferguson-Miller,S
摘要：以马细胞色素c-Sepharose4B为基质，采用亲和层析法从大鼠肝脏和牛心中纯化细胞色素氧化酶。这一方法的成功归功于酶与非离子去污剂的彻底分散以及细胞色素c的赖氨酸残基与溴化氰活化的琼脂糖之间的低密度交联。从用十二烷基麦芽糖苷溶解的线粒体膜中一步纯化牛肉心脏氧化酶，得到一种纯度与酵母细胞色素c基质相当的酶[Azzi，A.，Bill，K.，&Broger，C.(1982)Proc]。娜塔莉。阿卡德。SCI。以十二烷基麦芽糖苷为溶剂，用羟基磷灰石和马细胞色素C亲和层析法制备大鼠肝脏氧化酶，得到高纯度(血红素a/mg蛋白质12.5~13.5nmoL)、高活性(TN)的酶
D. A. Thompson and S. Ferguson-Miller* abstract: Cytochrome oxidase is purified from rat liver and beef heart by affinity chromatography on a matrix of horse cytochrome c-Sepharose 4B. The success of this procedure, which employs a matrix previously found ineffectivewith beef or yeast oxidase, is attributed to thorough dispersion of the enzyme with nonionicdetergent and a low density of cross-linking between the lysine residues of cytochrome c and the cyanogen bromide activated Sepharose. Beef heart oxidase is purified in one step from mitochondrial membranes solu-bilized with lauryl maltoside, yielding an enzyme of purity comparable to that obtained on a yeast cytochrome c matrix [Azzi, A., Bill, K., & Broger, C.(1982) Proc. Natl. Acad. Sci. USA 79, 2447-2450], Rat liver oxidase is prepared by hydroxyapatite and horse cytochrome c affinity chromatography in lauryl maltoside, yielding enzyme of high purity (12.5-13.5 nmol of heme a/mg of protein), high activity (TN