Enhancement of aniline hydroxylation in human liver microsomes.
Effects of cyanide, acetone, 2,2'-bipyridine and paraoxon on aniline hydroxylation by human liver microsomes were studied. The activity of aniline hydroxylation was inhibited by cyanide when low concentrations of substrate were used, whereas the activity was increased by the addition of cyanide when higher concentrations of substrate were used. Although there were large variences among different liver samples in the extent of the activation of aniline hydroxylation, acetone, 2,2'-bipyridine and paraoxon also exerted stimulatory effects on aniline hydroxylation in human liver microsomes. The degree of the stimulation was not related with the activities observed in the absence of these compounds.
Kitada
M
M
Hasunuma
Y
Y
Rikihisa
T
T
Kanakubo
Y
Y
D015082:2,2'-Dipyridyl / Q000494:pharmacology; D000096:Acetone / Q000494:pharmacology; D000328:Adult; D000814:Aniline Compounds / Q000378:metabolism*; D002648:Child; D002675:Child, Preschool; D003486:Cyanides / Q000494:pharmacology; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism; D005260:Female; D006801:Humans; D006900:Hydroxylation; D066298:In Vitro Techniques; D007700:Kinetics; D008297:Male; D008862:Microsomes, Liver / Q000378:metabolism*; D008875:Middle Aged; D009251:NADPH-Ferrihemoprotein Reductase / Q000378:metabolism; D010261:Paraoxon / Q000494:pharmacology
D000814:Aniline Compounds; D003486:Cyanides; D000096:Acetone; D015082:2,2'-Dipyridyl; D003577:Cytochrome P-450 Enzyme System; D009251:NADPH-Ferrihemoprotein Reductase; D010261:Paraoxon