Characterization of some monooxygenase activities and solubilization of hepatic cytochrome P-450 in two species of freshwater fish, the nase (Chondrostoma nasus) and the roach (Rutilus rutilus).
1. Hepatic monooxygenase activities were studied in microsomal fractions from two species of freshwater fish, the nase (Chondrostoma nasus) and the European roach (Rutilus rutilus). 2. These activities were determined by using four substrates, 7-ethoxycoumarin, 7-ethoxyresorufin, benzo(a)pyrene, and 2,5-diphenyloxazole and were characterized according to pH, temperature, cofactors, and the differential effects of two inhibitors, metyrapone and alpha-naphthoflavone. 3. Solubilization of microsomes was achieved by the use of detergents, with a good recovery of the cytochrome P-450.
D000818:Animals; D003530:Cyprinidae / Q000378:metabolism*; D003577:Cytochrome P-450 Enzyme System / Q000302:isolation & purification / Q000378:metabolism*; D005399:Fishes / Q000378:metabolism*; D005618:Fresh Water; D007700:Kinetics; D008862:Microsomes, Liver / Q000201:enzymology*; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D009251:NADPH-Ferrihemoprotein Reductase / Q000378:metabolism; D012995:Solubility; D013045:Species Specificity
D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D009251:NADPH-Ferrihemoprotein Reductase