Nicotinamide-adenine dinucleotide-methemoglobin reductase activity in erythrocytes from cats.
Reduced nicotinamide-adenine dinucleotide (NADH)-methemoglobin reductase activity in feline erythrocyte lysates was determined, using potassium ferricyanide as substrate. The optimum conditions for the assay were pH 8 and 37 C. Mean NADH-ferricyanide reductase activity in cats was 15.7 +/- 4.1 mumoles of substrate converted/g of hemoglobin/min. The migration of NADH-ferricyanide reductase was similar to that of the NADH-methemoglobin reductase (NADH diaphorase) on starch gel electrophoresis.
D000818:Animals; D002415:Cats / Q000097:blood*; D042966:Cytochrome-B(5) Reductase / Q000097:blood*; D004592:Electrophoresis, Starch Gel; D004912:Erythrocytes / Q000201:enzymology*; D005292:Ferricyanides; D006863:Hydrogen-Ion Concentration; D009247:NADH, NADPH Oxidoreductases / Q000097:blood*
D005292:Ferricyanides; D009247:NADH, NADPH Oxidoreductases; D042966:Cytochrome-B(5) Reductase; C014227:ferricyanide reductase; C028033:potassium ferricyanide