INVOLVEMENT OF LIVER ALDEHYDE OXIDASE IN CONVERSION OF N-HYDROXYURETHANE TO URETHANE
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概要
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The present study provides the evidence that liver aldehyde oxidase in the presence of its electron donors can catalyze the reduction of N-hydroxyurethane ot urethane under anaerobic conditions. Guinea pig liver 9000×g supernatant and cytosol, but not liver microsomes, exhibited N-hydroxyurethane reductase activity in the presence of acetaldehyde or 2-hydroxypyrimidine. The cytosolic enzyme was precipitated with ammonium sulfate between 30 and 45% ammonium sulfate saturation. The N-hydroxyurethane reductase and aldehyde oxidase activities of the precipitate were similarly susceptible to inhibition by a variety of chemicals. When the precipitate was chromatographed on a DEAE-cellulose column, the elution peak position of N-hydroxyurethane reductase was entirely identical with that of aldehyde oxidase. Furthermore, purified rabbit liver aldehyde oxidase also exhibited a significant N-hydroxyurethane reductase activity in the presence of acetaldehyde or 2-hydroxypyrimidine.
- 公益社団法人日本薬学会の論文
著者
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KITAMURA Shigeyuki
Institute of Pharmaceutical Science, Hiroshima University School of Medicine
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TATSUMI Kiyoshi
Institute of Pharmaceutical Science, Hiroshima University School of Medicine
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Tatsumi Kiyoshi
Institute Of Pharmaceutical Science Hiroshima University School Of Medicine
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Tatsumi Kiyoshi
Institute Of Pharmaceutical Science. Hiroshima University School Of Medicine
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Sugihara Kazumi
Institute Of Pharmaceutical Science Hiroshima University School Of Medicine
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Kitamura Shigeyuki
Institute Of Pharmaceutical Science Hiroshima University School Of Medicine
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Kitamura Shigeyuki
Institute Of Pharmaceutical Sciences Hiroshima University School Of Medicine
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Kitamura Shigeyuki
Institute Of Pharmaceutical Science. Hiroshima University School Of Medicine
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Sugihara Kazumi
Institute Of Pharmaceutical Science. Hiroshima University School Of Medicine
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