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+.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Aldehyde Reductase* / antagonists & inhibitors
-
Aldehyde Reductase* / isolation & purification
-
Aldehyde Reductase* / metabolism
-
Amino Acids / analysis
-
Animals
-
Cattle
-
Chromatography, Affinity
-
Glucose / metabolism
-
Glyceraldehyde / metabolism
-
Kinetics
-
Lens, Crystalline / enzymology*
-
Molecular Weight
-
NADP / metabolism
-
Osmolar Concentration
-
Substrate Specificity
-
Sugar Alcohol Dehydrogenases* / isolation & purification
-
Sugar Alcohol Dehydrogenases* / metabolism
Substances
-
Amino Acids
-
Glyceraldehyde
-
NADP
-
Sugar Alcohol Dehydrogenases
-
Aldehyde Reductase
-
Glucose