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  • Title: Bovine lens aldehyde reductase (aldose reductase). Purification, kinetics and mechanism.
    Author: Halder AB, Crabbe MJ.
    Journal: Biochem J; 1984 Apr 01; 219(1):33-9. PubMed ID: 6426471.
    Abstract:
    Aldehyde reductase (aldose reductase) was purified to homogeneity (as judged by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis) from bovine lens by affinity chromatography on NADP+-Sepharose. The enzyme, a monomer of Mr about 40000, was active with a variety of alpha- hydroxyketones , including fructose. The minimum degree of the rate equation was 2:2 in the case of DL-glyceraldehyde, but linear kinetics were observed for glucose and NADPH over the concentration range studied. The enzyme largely followed a ternary-complex mechanism, with initial binding of NADPH before glucose and final release of NADP+.
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