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  • Title: Lens aldo-keto reductase of Camelus dromedarius: purification and properties.
    Author: Del Corso A, Barsacchi D, Osman AM, Mohamed AS, Tozzi MG, Camici M, Mura U.
    Journal: Biochim Biophys Acta; 1989 Oct 13; 993(1):116-20. PubMed ID: 2679888.
    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.
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