NAD(P)H dehydrogenase from rabbit and rat liver: purification and some properties.
NAD(P)H dehydrogenase from rabbit liver was purified to electrophoretic homogeneity using a procedure also found applicable for the rat liver enzyme. Rabbit and rat liver enzymes showed different behaviour in isoelectric focusing and different Km values and turnover numbers. Both enzymes were inhibited to similar extents by warfarin. The rabbit enzyme is composed of two subunits of mol. wt 27,000 and contained 1 FAD group per subunit. Some absorption and circular dichroism properties of the rat enzyme are shown.
D000818:Animals; D002847:Chromatography, Agarose; D002942:Circular Dichroism; D004228:Dithionitrobenzoic Acid / Q000494:pharmacology; D004586:Electrophoresis; D005260:Female; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D008297:Male; D008627:Mercuric Chloride / Q000494:pharmacology; D009247:NADH, NADPH Oxidoreductases / Q000302:isolation & purification*; D009252:NADPH Dehydrogenase / Q000032:analysis / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D011817:Rabbits; D051381:Rats; D014859:Warfarin / Q000494:pharmacology
D008627:Mercuric Chloride; D014859:Warfarin; D004228:Dithionitrobenzoic Acid; D009247:NADH, NADPH Oxidoreductases; D009252:NADPH Dehydrogenase