An analysis of the polypeptide composition of bovine heart mitochondrial NADH-ubiquinone oxidoreductase by two-dimensional polyacrylamide-gel electrophoresis.
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.
D000818:Animals; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D007106:Immune Sera; D007525:Isoelectric Focusing; D008929:Mitochondria, Heart / Q000201:enzymology*; D009247:NADH, NADPH Oxidoreductases / Q000276:immunology; D010455:Peptides / Q000032:analysis*; D011808:Quinone Reductases / Q000276:immunology; D013367:Submitochondrial Particles / Q000201:enzymology
D007106:Immune Sera; D010455:Peptides; D009247:NADH, NADPH Oxidoreductases; D011808:Quinone Reductases