title: THe formation of cytochrome P-450-metabolic intermediate complexes from amines, in the isolated perfused rat liver.
abstract: 1. Cytochrome P-450-metabolic intermediate (MI) complexes were formed from SKF 525-A, propoxyphene, acetylmethadol, noracetylmethadol, norbenzphetamine, and N-hydroxyamphetamine, but not methadone, in the isolated perfused rat liver. 2. The amount of MI complex from SKF 525-A (8% of the cytochrome P-450) after 1 h exceeded that for all other compounds (1--2%). 3. Both MI complex and residual substrate contributed to the inhibition of mixed-function oxidase activity observed. No substrate altered the total cytochrome P-450 concentration of NADPH-cytochrome c reductase activity. 4. The formation of MI complexes in isolated perfused liver corresponds to that seen in whole animals, and contrasts with that seen in microsomal preparations.
mesh_terms: D000588:Amines / Q000378:metabolism*; D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D066298:In Vitro Techniques; D008099:Liver / Q000378:metabolism*; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology; D006899:Mixed Function Oxygenases / Q000378:metabolism; D009251:NADPH-Ferrihemoprotein Reductase / Q000378:metabolism; D009575:Nitroanisole O-Demethylase / Q000378:metabolism; D051381:Rats; D013997:Time Factors
chemical_list: D000588:Amines; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D009575:Nitroanisole O-Demethylase; D009251:NADPH-Ferrihemoprotein Reductase