Properties of an aldose reductase from pig lens. Comparative studies of an aldehyde reductase from pig lens.

Item request has been placed! ×
Item request cannot be made. ×
loading   Processing Request
Read Online Read More Add to Saved list
  • Author(s): Branlant G
  • Source:
    European journal of biochemistry [Eur J Biochem] 1982 Dec; Vol. 129 (1), pp. 99-104.
  • Publication Type:
    Comparative Study; Journal Article
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID: 0107600 Publication Model: Print Cited Medium: Print ISSN: 0014-2956 (Print) Linking ISSN: 00142956 NLM ISO Abbreviation: Eur J Biochem Subsets: MEDLINE
    • Publication Information:
      Publication: -2004: Oxford, UK : Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
      Original Publication: Berlin, New York, Springer.
    • Subject Terms:
      Alcohol Oxidoreductases/*isolation & purification ; Aldehyde Reductase/*isolation & purification ; Lens, Crystalline/*enzymology ; Sugar Alcohol Dehydrogenases/*isolation & purification; Alcohol Oxidoreductases/metabolism ; Aldehyde Reductase/metabolism ; Animals ; Chemical Phenomena ; Chemistry ; Chemistry, Physical ; Dithionitrobenzoic Acid/pharmacology ; NADP/metabolism ; Substrate Specificity ; Swine ; Zinc/pharmacology
    • Abstract:
      Two monomeric NADPH enzymes from pig lens, an aldehyde reductase and an aldose reductase, have been characterized. The aldose reductase is obtained in a pure form. The aldehyde reductase, usually called hexonate dehydrogenase, is the same protein as that was recently isolated from pig liver [Branlant, G. and Biellmann, J.F. (1980) Eur. J. Biochem. 105, 611-621]. The aldose reductase is shown to have a number of properties in common with the aldehyde reductase, namely its physico-chemical properties, its tendency to be inhibited by quercitine derivatives and its substrate specificity. These two enzymes differ in their immunological properties. Only aldose reductase has a reactive Cys residue, localized in or near the substrate binding site. In contrast to that shown for aldehyde reductase [Branlant, G. et al. (1981) Eur. J. Biochem. 116, 505-512; Branlant, G. (1982) Eur. J. Biochem. 121, 407-411], no anion-recognition sites are in the substrate binding site of aldose reductase. The fact that also sugars are substrates for aldose reductase support the idea that this enzyme is implicated in the formation of sugar cataract as suggested by Kinoshita, J.H. et al. [J. Am. Med. Ass. 246, 257-261 (1981)]. Pig lens aldose reductase does not show homotropic cooperative effects with respect to either substrate or coenzyme.
    • Accession Number:
      53-59-8 (NADP)
      9BZQ3U62JX (Dithionitrobenzoic Acid)
      EC 1.1.- (Alcohol Oxidoreductases)
      EC 1.1.- (Sugar Alcohol Dehydrogenases)
      EC 1.1.1.2 (alcohol dehydrogenase (NADP+))
      EC 1.1.1.21 (Aldehyde Reductase)
      J41CSQ7QDS (Zinc)
    • Publication Date:
      Date Created: 19821201 Date Completed: 19830407 Latest Revision: 20190620
    • Publication Date:
      20240829
    • Accession Number:
      10.1111/j.1432-1033.1982.tb07026.x
    • Accession Number:
      6819141