Kitamura S, Tatsumi K
Biochem Biophys Res Commun. 1984 Jun 29;121(3):749-54. doi: 10.1016/0006-291x(84)90742-3.
Reduction of tertiary amine N-oxides to the corresponding amines by liver preparations was investigated with imipramine N-oxide and cyclobenzaprine N-oxide under anaerobic conditions. Rabbit liver cytosol in the presence of an electron donor of aldehyde oxidase exhibited a significant N-oxide reductase activity which is comparable to the activity of the liver microsomes supplemented with NADPH. Rabbit liver aldehyde oxidase also exhibited the N-oxide reductase activity in the presence of its electron donor, indicating that the activity observed in the liver cytosol is due to this cytosolic enzyme. Furthermore, the tertiary amine N-oxide reductase activity of liver cytosols from rats, mice, hamsters and hogs was demonstrated by comparison with that of liver microsomes from these mammalian species.
在厌氧条件下,用丙咪嗪氮氧化物和环苯扎林氮氧化物研究了肝脏制剂将叔胺氮氧化物还原为相应胺类的情况。在醛氧化酶电子供体存在下,兔肝细胞溶胶表现出显著的氮氧化物还原酶活性,这与补充了NADPH的肝脏微粒体活性相当。兔肝脏醛氧化酶在其电子供体存在下也表现出氮氧化物还原酶活性,表明在肝细胞溶胶中观察到的活性归因于这种胞质酶。此外,通过与这些哺乳动物物种的肝脏微粒体活性进行比较,证实了大鼠、小鼠、仓鼠和猪肝脏胞质溶胶的叔胺氮氧化物还原酶活性。