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Purification and partial characterization of dimeric dihydrodiol dehydrogenase from monkey kidney.
Biochem Biophys Res Commun. 1987 Jun 30; 145(3):1260-6.BB

Abstract

Dihydrodiol dehydrogenase activity was detected in the cytosol of several monkey tissues, among which kidney exhibited the highest activity and contained a high-molecular weight (Mr approximately 65,000) enzyme species. The enzyme species was purified to apparent homogeneity and showed a subunit molecular weight of 39,000. The enzyme oxidized benzene dihydrodiol (Km = 0.9 mM) at a pH optimum of 9.8, and highly reduced vicinal diketones such as camphorquinone (Km = 0.1 mM) and diacetyl (Km = 0.8 mM) around pH 7.5, but alicyclic alcohols, hydroxysteroids and ketosteroids were inactive substrates for this enzyme. Quercitrin, SH-reagents, stilbestrol were inhibitory to the enzyme activity, but other synthetic estrogens, anti-inflammatory agents and 3-ketosteroids were not.

Authors

No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

3300644

Citation

Hara, A, et al. "Purification and Partial Characterization of Dimeric Dihydrodiol Dehydrogenase From Monkey Kidney." Biochemical and Biophysical Research Communications, vol. 145, no. 3, 1987, pp. 1260-6.
Hara A, Mouri K, Sawada H. Purification and partial characterization of dimeric dihydrodiol dehydrogenase from monkey kidney. Biochem Biophys Res Commun. 1987;145(3):1260-6.
Hara, A., Mouri, K., & Sawada, H. (1987). Purification and partial characterization of dimeric dihydrodiol dehydrogenase from monkey kidney. Biochemical and Biophysical Research Communications, 145(3), 1260-6.
Hara A, Mouri K, Sawada H. Purification and Partial Characterization of Dimeric Dihydrodiol Dehydrogenase From Monkey Kidney. Biochem Biophys Res Commun. 1987 Jun 30;145(3):1260-6. PubMed PMID: 3300644.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification and partial characterization of dimeric dihydrodiol dehydrogenase from monkey kidney. AU - Hara,A, AU - Mouri,K, AU - Sawada,H, PY - 1987/6/30/pubmed PY - 1987/6/30/medline PY - 1987/6/30/entrez SP - 1260 EP - 6 JF - Biochemical and biophysical research communications JO - Biochem. Biophys. Res. Commun. VL - 145 IS - 3 N2 - Dihydrodiol dehydrogenase activity was detected in the cytosol of several monkey tissues, among which kidney exhibited the highest activity and contained a high-molecular weight (Mr approximately 65,000) enzyme species. The enzyme species was purified to apparent homogeneity and showed a subunit molecular weight of 39,000. The enzyme oxidized benzene dihydrodiol (Km = 0.9 mM) at a pH optimum of 9.8, and highly reduced vicinal diketones such as camphorquinone (Km = 0.1 mM) and diacetyl (Km = 0.8 mM) around pH 7.5, but alicyclic alcohols, hydroxysteroids and ketosteroids were inactive substrates for this enzyme. Quercitrin, SH-reagents, stilbestrol were inhibitory to the enzyme activity, but other synthetic estrogens, anti-inflammatory agents and 3-ketosteroids were not. SN - 0006-291X UR - https://www.unboundmedicine.com/medline/citation/3300644/Purification_and_partial_characterization_of_dimeric_dihydrodiol_dehydrogenase_from_monkey_kidney_ L2 - https://linkinghub.elsevier.com/retrieve/pii/0006-291X(87)91573-7 DB - PRIME DP - Unbound Medicine ER -