Tags

Type your tag names separated by a space and hit enter

Purification and properties of two multiple forms of dihydrodiol dehydrogenase from guinea-pig testis.
Biochim Biophys Acta. 1987 Apr 08; 912(2):270-7.BB

Abstract

NADP+-dependent dihydrodiol dehydrogenase (trans-1,2-dihydrobenzene-1,2-diol: NADP+ oxidoreductase, EC 1.3.1.20) activity in the cytosol of guinea-pig testis was separated into two major and two minor peaks by Q-Sepharose chromatography; one minor form was immunologically cross-reacted with hepatic aldehyde reductase. The two major enzyme forms were purified to homogeneity. One form, which had the highest amount in the tissue, was a monomeric protein with a molecular weight of 32,000 and isoelectric point of 4.2, showed strict specificity for benzene dihydrodiol and NADP+, and reduced pyridine aldehydes, glyceraldehyde and diacetyl at low rates. Another form, with a molecular weight of 36,000 and isoelectric point of 5.0, oxidized n-butanol, glycerol and sorbitol as well as benzene dihydrodiol in the presence of NADP+ or NAD+, and exhibited much higher reductase activity towards various aldehydes, aldoses and diacetyl. The pI 5.0 form was more sensitive to inhibition by sorbinil and p-chloromercuriphenyl sulfonate than the pI 4.2 form and was activated by sulfate ion. The two enzymes did not catalyze the oxidation of hydroxysteroids and xenobiotic alicyclic alcohols and were immunologically different from hepatic 17 beta-hydroxysteroid-dihydrodiol dehydrogenase. The results indicate that guinea-pig testis contains at least two dihydrodiol dehydrogenases distinct from the hepatic enzymes, one of which, the pI 5.0 enzyme form, may be identical to aldose reductase.

Authors

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

3548826

Citation

Matsuura, K, et al. "Purification and Properties of Two Multiple Forms of Dihydrodiol Dehydrogenase From Guinea-pig Testis." Biochimica Et Biophysica Acta, vol. 912, no. 2, 1987, pp. 270-7.
Matsuura K, Hara A, Nakayama T, et al. Purification and properties of two multiple forms of dihydrodiol dehydrogenase from guinea-pig testis. Biochim Biophys Acta. 1987;912(2):270-7.
Matsuura, K., Hara, A., Nakayama, T., Nakagawa, M., & Sawada, H. (1987). Purification and properties of two multiple forms of dihydrodiol dehydrogenase from guinea-pig testis. Biochimica Et Biophysica Acta, 912(2), 270-7.
Matsuura K, et al. Purification and Properties of Two Multiple Forms of Dihydrodiol Dehydrogenase From Guinea-pig Testis. Biochim Biophys Acta. 1987 Apr 8;912(2):270-7. PubMed PMID: 3548826.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification and properties of two multiple forms of dihydrodiol dehydrogenase from guinea-pig testis. AU - Matsuura,K, AU - Hara,A, AU - Nakayama,T, AU - Nakagawa,M, AU - Sawada,H, PY - 1987/4/8/pubmed PY - 1987/4/8/medline PY - 1987/4/8/entrez SP - 270 EP - 7 JF - Biochimica et biophysica acta JO - Biochim. Biophys. Acta VL - 912 IS - 2 N2 - NADP+-dependent dihydrodiol dehydrogenase (trans-1,2-dihydrobenzene-1,2-diol: NADP+ oxidoreductase, EC 1.3.1.20) activity in the cytosol of guinea-pig testis was separated into two major and two minor peaks by Q-Sepharose chromatography; one minor form was immunologically cross-reacted with hepatic aldehyde reductase. The two major enzyme forms were purified to homogeneity. One form, which had the highest amount in the tissue, was a monomeric protein with a molecular weight of 32,000 and isoelectric point of 4.2, showed strict specificity for benzene dihydrodiol and NADP+, and reduced pyridine aldehydes, glyceraldehyde and diacetyl at low rates. Another form, with a molecular weight of 36,000 and isoelectric point of 5.0, oxidized n-butanol, glycerol and sorbitol as well as benzene dihydrodiol in the presence of NADP+ or NAD+, and exhibited much higher reductase activity towards various aldehydes, aldoses and diacetyl. The pI 5.0 form was more sensitive to inhibition by sorbinil and p-chloromercuriphenyl sulfonate than the pI 4.2 form and was activated by sulfate ion. The two enzymes did not catalyze the oxidation of hydroxysteroids and xenobiotic alicyclic alcohols and were immunologically different from hepatic 17 beta-hydroxysteroid-dihydrodiol dehydrogenase. The results indicate that guinea-pig testis contains at least two dihydrodiol dehydrogenases distinct from the hepatic enzymes, one of which, the pI 5.0 enzyme form, may be identical to aldose reductase. SN - 0006-3002 UR - https://www.unboundmedicine.com/medline/citation/3548826/Purification_and_properties_of_two_multiple_forms_of_dihydrodiol_dehydrogenase_from_guinea_pig_testis_ L2 - https://linkinghub.elsevier.com/retrieve/pii/0167-4838(87)90097-5 DB - PRIME DP - Unbound Medicine ER -