ANALYSIS OF THE POLYPEPTIDE COMPOSITION OF BOVINE HEART MITOCHONDRIAL NADH-UBIQUINONE OXIDOREDUCTASE BY 2-DIMENSIONAL POLYACRYLAMIDE-GEL ELECTROPHORESIS

被引：88
作者：
HERON, C
SMITH, S
RAGAN, CI
机构：
来源：
BIOCHEMICAL JOURNAL | 1979年 / 181卷 / 02期
关键词：
D O I：
10.1042/bj1810435
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Purified preparations of Complex I (NADH-ubiquinone oxidoreductase) from bovine heart mitochondria may be resolved into 26 polypeptides by two-dimensional analysis combining isoelectric focusing and polyacrylamide-gel electrophoresis in sodium dodecyl sulphate. Similar analyses of the fragments obtained from chaotropic resolution of the enzyme show that each of these fragments contains a distinct and non-overlapping set of polypeptides. Evidence that the polypeptides seen in the intact enzyme are true constituents comes from analyses of immunoprecipitates obtained by allowing Complex I or solubilized submitochondrial particles to react with antisera directed against the whole enzyme and a subfragment of the enzyme.
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收藏
页码：435 / 443
页数：9
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