Stanley J S, Benson A M
Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock 72205.
Biochem J. 1988 Nov 15;256(1):303-6. doi: 10.1042/bj2560303.
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.
研究了人、大鼠和小鼠肝脏胞质溶胶、纯化的小鼠谷胱甘肽转移酶以及雄性和雌性小鼠肝外器官胞质溶胶对4-硝基喹啉1-氧化物与谷胱甘肽的结合作用。在底物浓度为0.1 mM时,人肝脏胞质溶胶对4-硝基喹啉1-氧化物的结合效果与对1-氯-2,4-二硝基苯的结合效果一样好。由Yb1和Yf亚基组成的小鼠同工酶对4-硝基喹啉1-氧化物表现出高活性。人、大鼠和小鼠肝脏对该底物的活性与肝脏同工酶组成相关。