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Resolution of complex I and isolation of NADH dehydrogenase and an iron--sulfur protein.

作者信息

Galante Y M, Hatefi Y

出版信息

Methods Enzymol. 1978;53:15-21. doi: 10.1016/s0076-6879(78)53007-3.

DOI:10.1016/s0076-6879(78)53007-3
PMID:713834
Abstract
摘要

相似文献

1
Resolution of complex I and isolation of NADH dehydrogenase and an iron--sulfur protein.
Methods Enzymol. 1978;53:15-21. doi: 10.1016/s0076-6879(78)53007-3.
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The iron-sulfur protein of cytochrome bc1 complex. Its occurrence in the mitochondrial inner membrane in excess of the amount constituting the complex.细胞色素bc1复合物的铁硫蛋白。它在线粒体内膜中的存在量超过构成该复合物的量。
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Purification of three iron-sulfur proteins from the iron-protein fragment of mitochondrial NADH-ubiquinone oxidoreductase.从线粒体NADH-泛醌氧化还原酶的铁蛋白片段中纯化三种铁硫蛋白。
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Toluene dioxygenase: purification of an iron-sulfur protein by affinity chromatography.
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Purification, characterization and properties of an NADH oxidase from Desulfovibrio vulgaris (Hildenborough) and its coupling to adenylyl phosphosulfate reductase.来自普通脱硫弧菌（希登伯勒菌株）的NADH氧化酶的纯化、表征及性质及其与腺苷酰磷酸硫酸还原酶的偶联
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