[Activity of NADPH-dependent monooxygenase hydroxylating system of rat liver under the effect of tetramethylthiuramdisulfide].
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.
D000633:Aminopyrine N-Demethylase / Q000378:metabolism; D000815:Aniline Hydroxylase / Q000378:metabolism*; D000818:Animals; D001189:Aryl Hydrocarbon Hydroxylases / Q000378:metabolism*; D006900:Hydroxylation; D007700:Kinetics; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D008297:Male; D009251:NADPH-Ferrihemoprotein Reductase / Q000378:metabolism*; D051381:Rats
D000815:Aniline Hydroxylase; D001189:Aryl Hydrocarbon Hydroxylases; D000633:Aminopyrine N-Demethylase; D009251:NADPH-Ferrihemoprotein Reductase
Aktivnost' NADPH-zavisimoĭ monooksigenaznoĭ gidroksiliruiushcheĭ sistemy pecheni krys pri vozdeĭstvii tetrametiltiuramdisul'fida.