S-(-)-nicotine-1'-N-oxide reductase activity of rat liver aldehyde oxidase
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چکیده
منابع مشابه
Investigation of the arylnitroso reductase activity of pig liver aldehyde reductase.
The reduction of p-nitroso-N-dimethylaniline, p-nitroso-N-diethylaniline, p-nitrosophenol and p-nitroso-N-phenylaniline with NADPH in the presence of aldehyde reductases 1 and 2 is described. The reactivity of these nitroso substrates is increased by hydrophobic substituents and those promoting OH- elimination from the molecule of the reduced substrate. NN-Dimethylbenzoquinonedi-iminium cation ...
متن کاملRat Liver Aldehyde Dehydrogenase
From normal rat liver mitochondrial and microsomal fractions, 4 distinct aldehyde dehydrogenase isozymes with millimolar substrate K,,, values have been purified and characterized. Two isozymes were isolated from mitochondria and 2 from microsomes. A mitochondrial aldehyde dehydrogenase with a substrate K,,, in the micromolar range was also identified. Subunit molecular weights for all millimol...
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An enzyme catalyzing the reduction of S-(2,4-dichlorophenacyl)glutathione to 2',4'-dichloroacetophenone was purified to apparent homogeneity by ion exchange, gel filtration, and hydroxylapatite chromatography from rat hepatic cytosol. The molecular weight was 30,000-37,000. The enzyme is distinct from the glutathione S-transferases, mercaptopyruvate sulfurtransferase, and glyoxalase I. Substrat...
متن کاملAldehyde oxidase activity in fresh human skin.
Human aldehyde oxidase (AO) is a molybdoflavoenzyme that commonly oxidizes azaheterocycles in therapeutic drugs. Although high metabolic clearance by AO resulted in several drug failures, existing in vitro-in vivo correlations are often poor and the extrahepatic role of AO practically unknown. This study investigated enzymatic activity of AO in fresh human skin, the largest organ of the body, f...
متن کاملN-oxide reduction of quinoxaline-1,4-dioxides catalyzed by porcine aldehyde oxidase SsAOX1.
Quinoxaline-1,4-dioxides (QdNOs) are a class of quinoxaline derivatives that are widely used in humans or animals as drugs or feed additives. However, the metabolic mechanism, especially the involved enzymes, has not been reported in detail. In this study, the N-oxide reduction enzyme, porcine aldehyde oxidase SsAOX1 was identified and characterized. The SsAOX1 gene was cloned from pig liver th...
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ژورنال
عنوان ژورنال: IUBMB Life
سال: 1996
ISSN: 1521-6543
DOI: 10.1080/15216549600201113