Purification and Some Properties of Hamster Liver Aldehyde Oxidase
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概要
- 論文の詳細を見る
Aldehyde oxidase was purified from hamster liver cytosol by ammonium sulfate fractionation, chromatography on DEAE-cellulose and Phenyl-Toyopearl, and HPLC-gel filtration on TSK-gel G3000SW_<XL> column. The purified enzyme was homogeneous by the criterion of sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Its molecular weight was determined to be 144800 by SDS-PAGE and 288000 by HPLC gel filtration. The isoelectric point was pH 5.1. The apparent K_m and V_<max> for benzaldehyde and 2-hydroxypyrimidine were 19.0 and 4.4μM, and 165 and 211 nmol/min/mg protein, respectively. The benzaldehyde oxidase activity was markedly inhibited by menadione and chlorpromazine. The substrate specificity was different from those of the enzymes from other animals.
- 公益社団法人日本薬学会の論文
- 1999-11-15
著者
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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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Kitamura Shigeyuki
Institute Of Pharmaceutical Science Hiroshima University School Of Medicine
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KATSUMA Yasuko
Institute of Pharmaceutical Science, Hiroshima University School of Medicine
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TANAKA Chikage
Institute of Pharmaceutical Science, Hiroshima University School of Medicine
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Tanaka Chikage
Institute Of Pharmaceutical Science Hiroshima University School Of Medicine
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Katsuma Yasuko
Institute Of Pharmaceutical Science Hiroshima University School Of Medicine
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