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Separation and properties of multiple forms of dihydrodiol dehydrogenase from hamster liver.
Int J Biochem. 1989; 21(4):367-75.IJ

Abstract

1. Five multiple forms of dihydrodiol dehydrogenase (EC 1.3.1.20) with similar molecular weights of around 35,000 were purified from hamster liver cytosol. 2. All the enzymes oxidized trans-dihydrodiols of benzene and naphthalene and reduced various carbonyl compounds, but showed clear differences in specificities for other alcohols and cofactors, and in inhibitor sensitivity. 3. Two NADP+-dependent enzymes were immunologically identified with aldehyde reductase (EC 1.1.1.2) and 3 alpha-hydroxytsteroid dehydrogenase (EC 1.1.1.50). 4. The other enzymes with dual cofactor specificity oxidized xenobiotic alicyclic alcohols, and one of them was active on 3 alpha- and 17 beta-hydroxysteroids with NAD+ as a preferable cofactor.

Authors+Show Affiliations

Department of Biochemistry, Gifu Pharmaceutical University, Japan.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

2663565

Citation

Sawada, H, et al. "Separation and Properties of Multiple Forms of Dihydrodiol Dehydrogenase From Hamster Liver." The International Journal of Biochemistry, vol. 21, no. 4, 1989, pp. 367-75.
Sawada H, Hara A, Nakagawa M, et al. Separation and properties of multiple forms of dihydrodiol dehydrogenase from hamster liver. Int J Biochem. 1989;21(4):367-75.
Sawada, H., Hara, A., Nakagawa, M., Tsukada, F., Ohmura, M., & Matsuura, K. (1989). Separation and properties of multiple forms of dihydrodiol dehydrogenase from hamster liver. The International Journal of Biochemistry, 21(4), 367-75.
Sawada H, et al. Separation and Properties of Multiple Forms of Dihydrodiol Dehydrogenase From Hamster Liver. Int J Biochem. 1989;21(4):367-75. PubMed PMID: 2663565.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Separation and properties of multiple forms of dihydrodiol dehydrogenase from hamster liver. AU - Sawada,H, AU - Hara,A, AU - Nakagawa,M, AU - Tsukada,F, AU - Ohmura,M, AU - Matsuura,K, PY - 1989/1/1/pubmed PY - 1989/1/1/medline PY - 1989/1/1/entrez SP - 367 EP - 75 JF - The International journal of biochemistry JO - Int. J. Biochem. VL - 21 IS - 4 N2 - 1. Five multiple forms of dihydrodiol dehydrogenase (EC 1.3.1.20) with similar molecular weights of around 35,000 were purified from hamster liver cytosol. 2. All the enzymes oxidized trans-dihydrodiols of benzene and naphthalene and reduced various carbonyl compounds, but showed clear differences in specificities for other alcohols and cofactors, and in inhibitor sensitivity. 3. Two NADP+-dependent enzymes were immunologically identified with aldehyde reductase (EC 1.1.1.2) and 3 alpha-hydroxytsteroid dehydrogenase (EC 1.1.1.50). 4. The other enzymes with dual cofactor specificity oxidized xenobiotic alicyclic alcohols, and one of them was active on 3 alpha- and 17 beta-hydroxysteroids with NAD+ as a preferable cofactor. SN - 0020-711X UR - https://www.unboundmedicine.com/medline/citation/2663565/Separation_and_properties_of_multiple_forms_of_dihydrodiol_dehydrogenase_from_hamster_liver_ DB - PRIME DP - Unbound Medicine ER -