Role of mixed-function amine oxidases in N-hydroxylation of 2-acetamidofluorene by hamster liver microsomal preparations.
Pretreatment of hamsters with 3-methylcholanthrene (100mg/kg body wt.) 24h before death did not appreciably change the extent of N-oxide formation when hepatic microsomal preparations were incubated with NN-dimethylaniline as substrate. In contrast, the N-hydroxylation of 2-acetamidofluorene was increased severalfold in hepatic microsomal preparations from pretreated animals. Under these conditions there were no appreciable changes in cytochrome P-450 content and NADPH-cytochrome c reductase activity. On the basis of these comparative data, it is suggested that amine oxidase is not involved in N-hydroxylation of 2-acetamidofluorene.
D000081:Acetamides / Q000378:metabolism; D000818:Animals; D006224:Cricetinae; D003577:Cytochrome P-450 Enzyme System; D005449:Fluorenes / Q000378:metabolism*; D006900:Hydroxylation; D008099:Liver / Q000201:enzymology; D008297:Male; D008748:Methylcholanthrene / Q000494:pharmacology; D008862:Microsomes, Liver / Q000187:drug effects / Q000201:enzymology / Q000378:metabolism*; D008995:Monoamine Oxidase / Q000378:metabolism*; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism
D000081:Acetamides; D005449:Fluorenes; D008748:Methylcholanthrene; D003577:Cytochrome P-450 Enzyme System; D008995:Monoamine Oxidase; D009247:NADH, NADPH Oxidoreductases