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Ukr Biokhim Zh (1978) ; 55(5): 574-6, 1983.
Article in Russian | MEDLINE | ID: mdl-6415882

ABSTRACT

Changes in the activity of a NADPH-dependent monooxygenase system of the rat liver are studied under the effect of tetramethylthiuramdisulphide. Under these conditions aniline hydroxylation is shown to be inhibited to a higher extent than amidopyrine demethylation. Besides a decrease in the level of cytochrome P-450, the central component of the microsomal system of hydroxylation, there appears cytochrome P-420--an inactivated form of cytochrome P-450.


Subject(s)
Aniline Hydroxylase/metabolism , Aryl Hydrocarbon Hydroxylases/metabolism , Liver/enzymology , NADPH-Ferrihemoprotein Reductase/metabolism , Aminopyrine N-Demethylase/metabolism , Animals , Hydroxylation , Kinetics , Liver/drug effects , Male , Rats
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