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. 1984 Apr 1;219(1):33–39. doi: 10.1042/bj2190033

Bovine lens aldehyde reductase (aldose reductase). Purification, kinetics and mechanism.

A B Halder, M J Crabbe
PMCID: PMC1153445  PMID: 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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Selected References

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