The conjugation of 4-nitroquinoline 1-oxide, a potent carcinogen, by mammalian glutathione transferases. 4-Nitroquinoline 1-oxide conjugation by human, rat and mouse liver cytosols, extrahepatic organs of mice and purified mouse glutathione transferase isoenzymes.
The conjugation of 4-nitroquinoline 1-oxide with GSH by human, rat and mouse liver cytosols, by purified mouse GSH transferases and by extrahepatic organ cytosols of male and female mice was investigated. 4-Nitroquinoline 1-oxide was as effectively conjugated by human liver cytosol as was 1-chloro-2,4-dinitrobenzene, at a substrate concentration of 0.1 mM. Mouse isoenzymes composed of Yb1 and Yf subunits exhibited high activity towards 4-nitroquinoline 1-oxide. Human, rat and mouse hepatic activities towards this substrate correlated with the hepatic isoenzyme compositions.
Stanley
J S
JS
Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock 72205.
Benson
A M
AM
D015112:4-Nitroquinoline-1-oxide / Q000378:metabolism*; D000818:Animals; D003600:Cytosol / Q000378:metabolism; D005260:Female; D005982:Glutathione Transferase / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D007527:Isoenzymes / Q000378:metabolism*; D008099:Liver / Q000378:metabolism*; D008297:Male; D051379:Mice; D009600:Nitroquinolines / Q000378:metabolism*; D051381:Rats; D013045:Species Specificity; D014018:Tissue Distribution
D007527:Isoenzymes; D009600:Nitroquinolines; D015112:4-Nitroquinoline-1-oxide; D005982:Glutathione Transferase