title: Lens aldo-keto reductase of Camelus dromedarius: purification and properties.
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 Mr = 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.
authors.affiliation: Department of Physiology and Biochemistry, University of Pisa, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Del Corso
authors.forename: D
authors.initials: D
authors.lastname: Barsacchi
authors.forename: A M
authors.initials: AM
authors.lastname: Osman
authors.forename: A S
authors.initials: AS
authors.lastname: Mohamed
authors.forename: M G
authors.initials: MG
authors.lastname: Tozzi
authors.forename: M
authors.initials: M
authors.lastname: Camici
authors.forename: U
authors.initials: U
authors.lastname: Mura
mesh_terms: D000429:Alcohol Oxidoreductases / Q000302:isolation & purification* / Q000378:metabolism; D000449:Aldehyde Reductase; D000074408:Aldo-Keto Reductases; D000818:Animals; D002162:Camelus; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D007908:Lens, Crystalline / Q000201:enzymology*; D008970:Molecular Weight; D013379:Substrate Specificity; D013816:Thermodynamics
chemical_list: D000429:Alcohol Oxidoreductases; D000074408:Aldo-Keto Reductases; D000449:Aldehyde Reductase