Tags

Type your tag names separated by a space and hit enter

Distribution and characterization of dihydrodiol dehydrogenases in mammalian ocular tissues.
Biochem J. 1991 Apr 01; 275 (Pt 1):113-9.BJ

Abstract

The immunological relationship of two forms of dihydrodiol dehydrogenase (DD) in pig lens to pig muscle aldose reductase and kidney aldehyde reductase has been studied. Although the minor enzyme form, a monomer of Mr 35,000, was identical with aldose reductase, the major enzyme form, a dimer of Mr 65,000, was distinct from the two reductases. The two enzyme species, although their amounts were low, were distributed in the cornea, iris-ciliary body, retina and choroid of the pig eye. In other mammals, rabbit lens exhibited much higher DD activity than did lens of mice, rats, cats, hamsters, guinea pigs and monkeys, and contained large amounts of the Mr-65,000 enzyme form as well as the minor enzyme form of Mr 35,000. In contrast, only the Mr-35,000 form of the enzyme was found in the lens of other species, except that a small amount of the high-Mr enzyme was detected in mouse lens. The high-Mr enzyme, purified from rabbit lens, was functionally and immunologically similar to dimeric DD of pig lens. The low-Mr enzyme forms, isolated or partially purified from these animal lenses, showed several features in common with aldose reductases from mammalian tissues. The dimeric enzymes of pig and rabbit lenses were NADP(+)-specific, whereas the low-Mr enzymes exhibited dual cofactor specificity and their activities with NAD+ were more than 3-fold higher than those with NADP+.

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 availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article

Language

eng

PubMed ID

2018467

Citation

Hara, A, et al. "Distribution and Characterization of Dihydrodiol Dehydrogenases in Mammalian Ocular Tissues." The Biochemical Journal, vol. 275 (Pt 1), 1991, pp. 113-9.
Hara A, Nakayama T, Harada T, et al. Distribution and characterization of dihydrodiol dehydrogenases in mammalian ocular tissues. Biochem J. 1991;275 (Pt 1):113-9.
Hara, A., Nakayama, T., Harada, T., Kanazu, T., Shinoda, M., Deyashiki, Y., & Sawada, H. (1991). Distribution and characterization of dihydrodiol dehydrogenases in mammalian ocular tissues. The Biochemical Journal, 275 (Pt 1), 113-9.
Hara A, et al. Distribution and Characterization of Dihydrodiol Dehydrogenases in Mammalian Ocular Tissues. Biochem J. 1991 Apr 1;275 (Pt 1):113-9. PubMed PMID: 2018467.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Distribution and characterization of dihydrodiol dehydrogenases in mammalian ocular tissues. AU - Hara,A, AU - Nakayama,T, AU - Harada,T, AU - Kanazu,T, AU - Shinoda,M, AU - Deyashiki,Y, AU - Sawada,H, PY - 1991/4/1/pubmed PY - 1991/4/1/medline PY - 1991/4/1/entrez SP - 113 EP - 9 JF - The Biochemical journal JO - Biochem. J. VL - 275 (Pt 1) N2 - The immunological relationship of two forms of dihydrodiol dehydrogenase (DD) in pig lens to pig muscle aldose reductase and kidney aldehyde reductase has been studied. Although the minor enzyme form, a monomer of Mr 35,000, was identical with aldose reductase, the major enzyme form, a dimer of Mr 65,000, was distinct from the two reductases. The two enzyme species, although their amounts were low, were distributed in the cornea, iris-ciliary body, retina and choroid of the pig eye. In other mammals, rabbit lens exhibited much higher DD activity than did lens of mice, rats, cats, hamsters, guinea pigs and monkeys, and contained large amounts of the Mr-65,000 enzyme form as well as the minor enzyme form of Mr 35,000. In contrast, only the Mr-35,000 form of the enzyme was found in the lens of other species, except that a small amount of the high-Mr enzyme was detected in mouse lens. The high-Mr enzyme, purified from rabbit lens, was functionally and immunologically similar to dimeric DD of pig lens. The low-Mr enzyme forms, isolated or partially purified from these animal lenses, showed several features in common with aldose reductases from mammalian tissues. The dimeric enzymes of pig and rabbit lenses were NADP(+)-specific, whereas the low-Mr enzymes exhibited dual cofactor specificity and their activities with NAD+ were more than 3-fold higher than those with NADP+. SN - 0264-6021 UR - https://www.unboundmedicine.com/medline/citation/2018467/Distribution_and_characterization_of_dihydrodiol_dehydrogenases_in_mammalian_ocular_tissues_ L2 - https://portlandpress.com/biochemj/article-lookup/doi/10.1042/bj2750113 DB - PRIME DP - Unbound Medicine ER -