Isolation and characterization of a NADH-dehydrogenase from rat liver mitochondria.
Mitochondrial NADH dehydrogenase has been purified from rat liver mitochondria by protamine sulfate fractionation and DEAE-Sephadex chromatography. The enzyme is water-soluble and its molecular weight has been estimated at 400 +/- 50 kilodaltons. NADH-ferricyanide reductase and NADH cytochrome c reductase activities have been studied and the kinetic parameters have been determined. Both substrates, NADH and the electron acceptor (ferricyanide or cytochrome c) have an inhibitor effect on the reductase activities and the kinetic mechanism of the enzyme is ping-pong bi-bi.
D000818:Animals; D002852:Chromatography, Ion Exchange; D003579:Cytochrome Reductases / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008930:Mitochondria, Liver / Q000201:enzymology*; D009245:NADH Dehydrogenase / Q000302:isolation & purification* / Q000378:metabolism; D051381:Rats
D003579:Cytochrome Reductases; D009245:NADH Dehydrogenase