Chemical Modification Studies on Purified Bovine Lens Aldose Reductase
- 1 January 1985
- journal article
- research article
- Published by S. Karger AG in Ophthalmic Research
- Vol. 17 (3) , 185-188
- https://doi.org/10.1159/000265372
Abstract
Chemical modification studies on homogeneous bovine lens aldose reductase using diethylpyrocarbonate, phenylglyoxal, butanedione. N-ethylmaleimide and p-chloromercuribenzoate indicate that histidine and arginine residues located at or near the nucleotide binding site may be important in binding or orientation of the NADPH, and that NADPH oxidation with glucose requires protein thiol.Keywords
This publication has 8 references indexed in Scilit:
- Bovine lens aldehyde reductase (aldose reductase). Purification, kinetics and mechanismBiochemical Journal, 1984
- The autoxidation of glyceraldehyde and other simple monosaccharides under physiological conditions catalysed by buffer ionsBiochimica et Biophysica Acta (BBA) - General Subjects, 1984
- A reaction mechanism for aldose reductase from lensBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- 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
- Presence of one essential arginine that specifically binds the 2′-phosphate of NADPH on each of the ketoacyl reductase and enoyl reductase active sites of fatty acid synthetaseArchives of Biochemistry and Biophysics, 1980
- Physical and kinetic properties of homogenous bovine lens aldose reductase.Journal of Biological Chemistry, 1976
- [44] Nitration with tetranitromethanePublished by Elsevier ,1972