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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

These references are in PubMed. This may not be the complete list of references from this article.

  1. Axén R., Porath J., Ernback S. Chemical coupling of peptides and proteins to polysaccharides by means of cyanogen halides. Nature. 1967 Jun 24;214(5095):1302–1304. doi: 10.1038/2141302a0. [DOI] [PubMed] [Google Scholar]
  2. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  3. Conrad S. M., Doughty C. C. Comparative studies on aldose reductase from bovine, rat and human lens. Biochim Biophys Acta. 1982 Nov 19;708(3):348–357. doi: 10.1016/0167-4838(82)90448-4. [DOI] [PubMed] [Google Scholar]
  4. Crabbe M. J. An enzyme kinetics program for desk-top computers. Comput Biol Med. 1982;12(4):263–283. doi: 10.1016/0010-4825(82)90031-2. [DOI] [PubMed] [Google Scholar]
  5. Crabbe M. J., Wolff S., Halder A. B., Ting H. H. Diabetic cataracts- is aldose reductase important? Metab Pediatr Ophthalmol. 1981;5(1):33–38. [PubMed] [Google Scholar]
  6. Cromlish J. A., Flynn T. G. Purification and characterization of an enzymically active cleavage product of pig kidney aldehyde reductase. Biochem J. 1983 Mar 1;209(3):597–607. doi: 10.1042/bj2090597. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Datiles M., Fukui H., Kuwabara T., Kinoshita J. H. Galactose cataract prevention with sorbinil, an aldose reductase inhibitor: a light microscopic study. Invest Ophthalmol Vis Sci. 1982 Feb;22(2):174–179. [PubMed] [Google Scholar]
  8. Doughty C. C., Conrad S. M. A reaction mechanism for aldose reductase from lens. Biochim Biophys Acta. 1982 Nov 19;708(3):358–364. doi: 10.1016/0167-4838(82)90449-6. [DOI] [PubMed] [Google Scholar]
  9. Jedziniak J. A., Chylack L. T., Jr, Cheng H. M., Gillis M. K., Kalustian A. A., Tung W. H. The sorbitol pathway in the human lens: aldose reductase and polyol dehydrogenase. Invest Ophthalmol Vis Sci. 1981 Mar;20(3):314–326. [PubMed] [Google Scholar]
  10. LOWRY O. H., PASSONNEAU J. V., ROCK M. K. The stability of pyridine nucleotides. J Biol Chem. 1961 Oct;236:2756–2759. [PubMed] [Google Scholar]
  11. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  12. Laemmli U. K., Favre M. Maturation of the head of bacteriophage T4. I. DNA packaging events. J Mol Biol. 1973 Nov 15;80(4):575–599. doi: 10.1016/0022-2836(73)90198-8. [DOI] [PubMed] [Google Scholar]
  13. Mosbach K., Guilford H., Ohlsson R., Scott M. General ligands in affinity chromatography. Cofactor-substrate elution of enzymes bound to the immobilized nucleotides adenosine 5'-monophosphate and nicotinamide-adenine dinucleotide. Biochem J. 1972 May;127(4):625–631. doi: 10.1042/bj1270625. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Sheaff C. M., Doughty C. C. Physical and kinetic properties of homogenous bovine lens aldose reductase. J Biol Chem. 1976 May 10;251(9):2696–2702. [PubMed] [Google Scholar]
  15. Thornalley P. J., Wolff S. P., Crabbe M. J., Stern A. The oxidation of oxyhaemoglobin by glyceraldehyde and other simple monosaccharides. Biochem J. 1984 Feb 1;217(3):615–622. doi: 10.1042/bj2170615. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Ting H. H., Crabbe M. J. Bovine lens aldehyde dehydrogenase. Purification and preliminary characterization. Biochem J. 1983 Nov 1;215(2):351–359. doi: 10.1042/bj2150351. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Varma S. D., Kinoshita J. H. The absence of cataracts in mice with congenital hyperglycemia. Exp Eye Res. 1974 Dec;19(6):577–582. doi: 10.1016/0014-4835(74)90095-5. [DOI] [PubMed] [Google Scholar]

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