TISSUE DISTRIBUTION AND CHARACTERISTICS OF XANTHINE OXIDASE AND ALLOPURINOL OXIDIZING ENZYME
スポンサーリンク
概要
- 論文の詳細を見る
Tissue distribution and levels of allopurinol oxidizing enzyme and xanthine oxidase with hypoxanthine as a substrate were compared with supernatant fractions from various tissues of mice and from liver of mice, rats, guinea pigs and rabbits. The allopurinol oxidizing enzyme activities in liver were quite different among the species and the sex difference of the enzyme activity existed only in mouse liver. In mice, the highest activity of allopurinol oxidizing enzyme was found in the liver with a trace value in lung, but the enzyme activity was not detected in brain, small intestine and kidney, while the highest activity of xanthine oxidase was detected in small intestine, lung, liver and kidney in that sequence. The allopurinol oxidizing enzyme activity in mouse liver supernatant fraction did not change after storage at -20°C or dialysis against 0.1 M Tris-HCl containing 1.15 % KCl, but the activity markedly decreased after dialysis against 0.1 M Tris-HCl. On the contrary, the xanthine oxidase was activated 2 to 3 times the usual activity after storage at -20°C or dialysis of the enzyme preparation. These results indicated that allopurinol was hydroxylated to oxipurinol mainly by the enzyme which is not identical to xanthine oxidase <I>in vivo</I>. A possible role of aldehyde oxidase involved in the allopurinol oxidation in liver supernatant fraction was discussed.
著者
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Yamamoto Itaru
Department Of Immunochemistry Faculty Of Pharmaceutical Science Okayama University
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Gohda Eiichi
Department Of Immunochemistry Division Of Pharmaceutical Sciences Okayama University Graduate School
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Iwata Heitaroh
Department Of Pharmacology Faculty Of Pharmaceutical Sciences Osaka University
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HUH Keun
Department of Pharmacology, Faculty of Pharmaceutical Sciences, Osaka University
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GOHDA Eiichi
Department of Biochemistry, Faculty of Dentistry, Osaka University
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