The antitubercular agent Pyrazinamide (PZA) binds to oxidized and reduced rat liver microsomal cytochrome P-450 with the binding characteristics typical of basic heterocyclic compounds. The PZA-cytochrome P-450(Fe2+) interaction, although characterized by rather weak affinity (Ks = 4 × 10-3M), has a PZA-cytochrome P-450(Fe2+) bond of considerable strenght and stability. PZA has an inhibitory effect on the aniline hydroxylase, p-nitroanisole O-demethylase and aminopyrine demethylase activities of rat liver microsomes. The PZA-cytochrome P-450(Fe2+) binding characteristics explain the observed inhibitory effect of the drug on the monooxygenase activities.
The inhibitory effect of pyrazinamide on microsomal monooxygenase activities is related to the binding to reduced cytochrome P-450 / R. Maffei Facino, M. Carini. - In: PHARMACOLOGICAL RESEARCH COMMUNICATIONS. - ISSN 0031-6989. - 12:6(1980), pp. 523-537.
The inhibitory effect of pyrazinamide on microsomal monooxygenase activities is related to the binding to reduced cytochrome P-450
R. Maffei FacinoPrimo
;M. CariniUltimo
1980
Abstract
The antitubercular agent Pyrazinamide (PZA) binds to oxidized and reduced rat liver microsomal cytochrome P-450 with the binding characteristics typical of basic heterocyclic compounds. The PZA-cytochrome P-450(Fe2+) interaction, although characterized by rather weak affinity (Ks = 4 × 10-3M), has a PZA-cytochrome P-450(Fe2+) bond of considerable strenght and stability. PZA has an inhibitory effect on the aniline hydroxylase, p-nitroanisole O-demethylase and aminopyrine demethylase activities of rat liver microsomes. The PZA-cytochrome P-450(Fe2+) binding characteristics explain the observed inhibitory effect of the drug on the monooxygenase activities.
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