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Title: Methemoglobin reductase activity in fish erythrocytes. Author: Scott EM, Harrington JP. Journal: Comp Biochem Physiol B; 1985; 82(3):511-3. PubMed ID: 4085211. Abstract: 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.[Abstract] [Full Text] [Related] [New Search]