Purification and some properties of aldose reductase from rabbit lens.

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Abstract
Four aldose reductases, designated as aldose reductases Ia, Ib, IIa and IIb, were purified to homogeneity from rabbit lens by a combination of several procedures such as ammonium sulfate precipitation, gel filtration, dye-affinity chromatography and chromatofocusing. The MW of the 4 aldose reductases were estimated to be 33,000 by Sephadex G-100 gel filtration, and to be 37,000 by SDS[sodium dodecyl sulfate]-polyacrylamide gel electrophoresis. These enzymes had an identical pH optimum of 5.6. Substrate specificity studies showed that the 4 enzymes were capable of reducing various aldehydes and aldoses. D-Hexoses (D-glucose and D-galactose) were poor substrates for aldose reductases IIa and IIb. Aldose reductases Ia and Ib used both NADH and NADPH as coenzymes, but aldose reductases IIa and IIb used NADPH specifically. Very high substrate concentrations were required to demonstrate the reaction in the reverse direction with these aldose reductases. Aldose reductases Ia and Ib were activated by SO4-, but aldose reductases IIa and IIb were not, and they were all inhibited remarkably by phenobarbital (1 mM). Aldose reductases Ia and Ib could be classified as aldose reductase (alditol:NADP+ oxidoreductase, EC 1.1.1.21).

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