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Isolation from pig lens of two proteins with dihydrodiol dehydrogenase and aldehyde reductase activities.
Biochem J. 1989 Dec 01; 264(2):403-7.BJ

Abstract

Dimeric and monomeric proteins containing dihydrodiol dehydrogenase and aldehyde reductase activities were purified from pig lens. The dimeric enzyme of Mr 65,000 specifically oxidized the trans-dihydrodiols of naphthalene and benzene with NADP+ as a strict cofactor, and reduced alpha-diketones, aromatic aldehydes and glyceraldehyde with NADPH as a cofactor. The monomeric enzyme of Mr 35,000, although identical with aldose reductase, oxidized the trans-dihydrodiol of naphthalene at a pH optimum of 7.6. These results suggest that the two enzymes are involved in the pathogenesis of naphthalene cataract.

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

2690827

Citation

Hara, A, et al. "Isolation From Pig Lens of Two Proteins With Dihydrodiol Dehydrogenase and Aldehyde Reductase Activities." The Biochemical Journal, vol. 264, no. 2, 1989, pp. 403-7.
Hara A, Harada T, Nakagawa M, et al. Isolation from pig lens of two proteins with dihydrodiol dehydrogenase and aldehyde reductase activities. Biochem J. 1989;264(2):403-7.
Hara, A., Harada, T., Nakagawa, M., Matsuura, K., Nakayama, T., & Sawada, H. (1989). Isolation from pig lens of two proteins with dihydrodiol dehydrogenase and aldehyde reductase activities. The Biochemical Journal, 264(2), 403-7.
Hara A, et al. Isolation From Pig Lens of Two Proteins With Dihydrodiol Dehydrogenase and Aldehyde Reductase Activities. Biochem J. 1989 Dec 1;264(2):403-7. PubMed PMID: 2690827.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Isolation from pig lens of two proteins with dihydrodiol dehydrogenase and aldehyde reductase activities. AU - Hara,A, AU - Harada,T, AU - Nakagawa,M, AU - Matsuura,K, AU - Nakayama,T, AU - Sawada,H, PY - 1989/12/1/pubmed PY - 1989/12/1/medline PY - 1989/12/1/entrez SP - 403 EP - 7 JF - The Biochemical journal JO - Biochem. J. VL - 264 IS - 2 N2 - Dimeric and monomeric proteins containing dihydrodiol dehydrogenase and aldehyde reductase activities were purified from pig lens. The dimeric enzyme of Mr 65,000 specifically oxidized the trans-dihydrodiols of naphthalene and benzene with NADP+ as a strict cofactor, and reduced alpha-diketones, aromatic aldehydes and glyceraldehyde with NADPH as a cofactor. The monomeric enzyme of Mr 35,000, although identical with aldose reductase, oxidized the trans-dihydrodiol of naphthalene at a pH optimum of 7.6. These results suggest that the two enzymes are involved in the pathogenesis of naphthalene cataract. SN - 0264-6021 UR - https://www.unboundmedicine.com/medline/citation/2690827/Isolation_from_pig_lens_of_two_proteins_with_dihydrodiol_dehydrogenase_and_aldehyde_reductase_activities_ L2 - https://portlandpress.com/biochemj/article-lookup/doi/10.1042/bj2640403 DB - PRIME DP - Unbound Medicine ER -