Bovine lens aldehyde reductase (aldose reductase). Purification, kinetics and mechanism.
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+.
D000449:Aldehyde Reductase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002846:Chromatography, Affinity; D005947:Glucose / Q000378:metabolism; D005985:Glyceraldehyde / Q000378:metabolism; D007700:Kinetics; D007908:Lens, Crystalline / Q000201:enzymology*; D008970:Molecular Weight; D009249:NADP / Q000378:metabolism; D009994:Osmolar Concentration; D013379:Substrate Specificity; D013401:Sugar Alcohol Dehydrogenases / Q000302:isolation & purification / Q000378:metabolism
D000596:Amino Acids; D005985:Glyceraldehyde; D009249:NADP; D013401:Sugar Alcohol Dehydrogenases; D000449:Aldehyde Reductase; D005947:Glucose