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- W2022182017 abstract "A series of dimethyltriazenes (Ar∙N=N∙NMe 2 ), monomethyltriazenes (Ar∙N=N∙NH∙Me), and triazene carbinolamines (Ar∙N=N∙NMe∙CH 2 OH) have been studied for their inhibitory effects on the enzyme, hog liver esterase (EC 3.1.1.1). p-Nitrophenyl acetate was used as the model substrate and the rate of hydrolysis was followed spectrophotometrically at 400 nm, the absorption maximum of the p-nitrophenylate ion. Only triazenes with an ester group in the aryl moiety exhibited significant inhibition. Preincubation of the enzyme with the monomethyltriazene (MeO 2 C∙C 6 H 4 ∙N=N∙NHMe) or the methyloltriazene (MeO 2 C∙C 6 H 4 ∙N=N∙NMe∙CH 2 OH) gave enhanced inhibition, which was not observed when the dimethyltriazene (MeO 2 C∙C 6 H 4 ∙N=N∙NMe 2 ) was preincubated with the enzyme. Inhibition of enzyme activity by the monomethyltriazene was shown to be essentially irreversible, whereas the model substrates, methyl benzoate and methyl p-aminobenzoate, gave reversible inhibition in the same assay. The inhibition by the N-methyloltriazene was only partially reversible. The results are discussed with relevance to the role of the monomethyltriazenes and N-methyloltriazenes as possible transportable metabolites of the antitumour dimethyltriazenes." @default.
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- W2022182017 date "1981-12-01" @default.
- W2022182017 modified "2023-10-18" @default.
- W2022182017 title "Triazene metabolism. II Transportability and enzyme inhibitory characteristics of metabolites of antitumor dimethyltriazenes" @default.
- W2022182017 doi "https://doi.org/10.1139/y81-194" @default.
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