Dihydrodiol dehydrogenases in guinea pig liver |
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| Authors: | A Hara K Hasebe M Hayashibara K Matsuura T Nakayama H Sawada |
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| Affiliation: | 1. College of Natural Resources and Environment, Northwest A&F University, Yangling 712100, Shaanxi, PR China;2. Key Laboratory of Plant Nutrition and the Agri-environment in Northwest China, Ministry of Agricultureand Rural Affairs, Yangling 712100, Shaanxi, PR China;3. State Key Laboratory of Urban Water Resource and Environment, Harbin Institute of Technology (SKLUWRE, HIT), Harbin 150090, PR China;4. Guangdong Provincial Research Center for Environment Pollution Control and Remediation Materials, Department of Ecology, College of Life Science and Technology, Jinan University, Guangzhou 510632, PR China;1. Department of Biophysics, The Health Science Center, Peking University, Beijing, 100191, China;2. Electron Microscopy Analysis Laboratory, The Health Science Center, Peking University, Beijing, 100191, China;3. Center for Protein Science, Peking University, Beijing, 100871, China;1. School of Pharmacy, Shanghai Jiao Tong University, Shanghai, 200240, China;2. China Research Center, DuPont Nutrition & Biosciences, Shanghai, 200335, China;1. Department of Applied Science and Technology, Anna University, Chennai, Tamil Nadu, 600025, India;2. Biofouling and Thermal Ecology Section, Water and Steam Chemistry Division, BARC Facilities, Kalpakkam, Tamil Nadu, 603102, India;3. Homi Bhabha National Institute, Mumbai, 400094, India |
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| Abstract: | Four major and four minor dihydrodiol dehydrogenases, with similar apparent molecular weights of 28,000 to 34,000 but with different charges, were purified from male guinea pig liver cytosol. One of the minor enzymes catalyzed only the oxidation of benzene dihydrodiol with a high Km value of 5.0 mM and was identified immunologically with aldehyde reductase. The other enzymes oxidized xenobiotic alicyclic alcohols and 17 beta-hydroxysteroids as well as benzene dihydrodiol. These enzymes exhibited higher affinity for 17 beta-hydroxysteroids than for alicyclic alcohols and benzene dihydrodiol, and immunologically cross-reacted with testosterone 17 beta-dehydrogenase purified from the same source. Four major enzymes and one minor with Km values for benzene dihydrodiol of about 0.2 mM, possessed specificity for 5 beta-androstane--17 beta-hydroxysteroids and dual cofactor requirement, whereas the other two minor enzymes with high Km values of over 5 mM showed apparent NADP and 5 alpha-androstane specificity. The dihydrodiol dehydrogenase activity was localized in the cytosol of liver. The results indicate that the hepatic oxidation of dihydrodiols in the guinea pig is mediated by cytosolic testosterone 17 beta-dehydrogenase isozymes and aldehyde reductase. Testosterone 17 beta-dehydrogenase immunologically identical to the liver enzymes was detected only in kidney, whereas aldehyde reductase was detected in all tissues of the guinea pig. |
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