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Lens aldo-keto reductase ofCamelus dromedarius: purification and properties

Authors
Journal
Biochimica et Biophysica Acta (BBA) - General Subjects
0304-4165
Publisher
Elsevier
Publication Date
Volume
993
Issue
1
Identifiers
DOI: 10.1016/0304-4165(89)90150-5
Keywords
  • Aldo-Keto Reductase
  • Lens
  • (C. Dromedarius)
Disciplines
  • Biology

Abstract

Abstract Aldo-keto reductase has been purified 13 000-fold from the lens of the camel ( Camelus dromedarius) to a specific activity of 85 U/mg protein. The enzyme is a monomeric protein, exhibiting a M r = 40 000 upon polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate. Camel lens aldo-keto reductase shows a broad substrate specificity, which is strictly dependent on NADPH, and is insensitive to inhibition by Sorbinil and valproate. Aldoses with a carbon chain with more than four residues, as well as glucuronate, are not reduced by the enzyme. On the basis of substrate specificity and sensitivity to inhibition, camel lens aldo-keto reductase appears to be distinct from the so far described aldose, aldehyde and carbonyl reductases.

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