Methemoglobin reductase activity in fish erythrocytes.
NADH-methemoglobin reductase activity of erythrocytes from the coho salmon, Oncorhynchus kisutch, sockeye salmon, Oncorhynchus nerka, and the rainbow trout, Salmo gairdneri exhibited a major band of activity that resembled the human enzyme in electrophoretic mobility. No polymorphism was found in 35 samples from rainbow trout, 4 samples from Dolly Varden, 29 samples from sockeye salmon, and 24 samples from coho salmon. All samples differed from the human enzyme in that they appeared to be membrane-bound and required the presence of a detergent, Triton X-100, for solubilization. Rainbow trout and coho salmon enzymatic activity is greater than the human enzyme activity at 15 degrees C.
D000818:Animals; D042966:Cytochrome-B(5) Reductase / Q000097:blood*; D004592:Electrophoresis, Starch Gel; D004912:Erythrocytes / Q000201:enzymology*; D005399:Fishes / Q000097:blood*; D009247:NADH, NADPH Oxidoreductases / Q000097:blood*; D012474:Salmon / Q000097:blood; D013045:Species Specificity; D014337:Trout / Q000097:blood; D014981:Xenopus / Q000097:blood
D009247:NADH, NADPH Oxidoreductases; D042966:Cytochrome-B(5) Reductase