Effects of butylated hydroxyanisole (BHA) and butylated hydroxytoluene (BHT) on metabolism of N,N-dimethyl-4-aminoazobenzene (DAB) by rat liver microsomes.
The antioxidants, BHA and BHT, inhibited the N-demethylation and ring hydroxylation of N,N-dimethyl-4-aminoazobenzene (DAB) by liver microsomes from untreated and phenobarbital (PB)-treated rats. BHA was somewhat more potent in this regard than was BHT. Microsomal NADPH oxidase from PB-treated rats was stimulated by BHA but control microsomal activity was unaffected. Glutathione did not appreciably reverse the inhibitory effect of BHA on DAB metabolism and had no effect on NADPH oxidase activity. It is concluded that inhibition of DAB metabolism by BHA cannot be accounted for by interaction with NADPH oxidase, particularly in untreated microsomes. It more likely affects one or more species of cytochrome P-450.
D000818:Animals; D000840:Anisoles / Q000494:pharmacology*; D002083:Butylated Hydroxyanisole / Q000494:pharmacology*; D002084:Butylated Hydroxytoluene / Q000494:pharmacology*; D003577:Cytochrome P-450 Enzyme System / Q000032:analysis; D066298:In Vitro Techniques; D008862:Microsomes, Liver / Q000378:metabolism*; D009247:NADH, NADPH Oxidoreductases / Q000032:analysis; D019255:NADPH Oxidases; D051381:Rats; D004124:p-Dimethylaminoazobenzene / Q000378:metabolism*
D000840:Anisoles; D002084:Butylated Hydroxytoluene; D002083:Butylated Hydroxyanisole; D003577:Cytochrome P-450 Enzyme System; D004124:p-Dimethylaminoazobenzene; D009247:NADH, NADPH Oxidoreductases; D019255:NADPH Oxidases