Induction of disopyramide N-dealkylation by phenobarbital and disopyramide in rat liver.
An in vitro assay for the determination of the activity of disopyramide-N-dealkylation was developed. This reaction was concluded to be catalyzed by the liver microsomal, cytochrome P-450 centered monooxygenase system. Phenobarbital enhanced the N-dealkylation of disopyramide four fold, and disopyramide itself 1.6 fold, whereas methylcholanthrene was without effect. Disopyramide also increased ethoxycoumarin deethylation 1.6 fold, and had a slight increasing effect on the activity of epoxide hydratase, but did not affect the activities of glutathione S-transferase or UDPglucuronosyltransferase.
D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism; D003640:Dealkylation; D004206:Disopyramide / Q000378:metabolism* / Q000494:pharmacology; D008099:Liver / Q000201:enzymology / Q000378:metabolism*; D008297:Male; D008748:Methylcholanthrene / Q000494:pharmacology; D008862:Microsomes, Liver / Q000378:metabolism; D006899:Mixed Function Oxygenases / Q000378:metabolism; D009245:NADH Dehydrogenase / Q000378:metabolism; D010634:Phenobarbital / Q000494:pharmacology*; D011725:Pyridines / Q000378:metabolism*; D051381:Rats
D011725:Pyridines; D008748:Methylcholanthrene; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D009245:NADH Dehydrogenase; D004206:Disopyramide; D010634:Phenobarbital