Chemical Modification Studies on Purified Bovine Lens Aldose Reductase

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.