Bovine lens aldehyde reductase (aldose reductase). Purification, kinetics and mechanism
- 1 April 1984
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 219 (1) , 33-39
- https://doi.org/10.1042/bj2190033
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+.This publication has 17 references indexed in Scilit:
- Comparative studies on aldose reductase from bovine, rat and human lensBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- GALACTOSE CATARACT PREVENTION WITH SORBINIL, AN ALDOSE REDUCTASE INHIBITOR - A LIGHT MICROSCOPIC STUDY1982
- DIABETIC CATARACTS - IS ALDOSE REDUCTASE IMPORTANT1981
- THE SORBITOL PATHWAY IN THE HUMAN LENS - ALDOSE REDUCTASE AND POLYOL DEHYDROGENASE1981
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- Physical and kinetic properties of homogenous bovine lens aldose reductase.Journal of Biological Chemistry, 1976
- The absence of cataracts in mice with congenital hyperglycemiaExperimental Eye Research, 1974
- Maturation of the head of bacteriophage T4Journal of Molecular Biology, 1973
- Chemical Coupling of Peptides and Proteins to Polysaccharides by Means of Cyanogen HalidesNature, 1967
- The Stability of Pyridine NucleotidesJournal of Biological Chemistry, 1961