Multiplicity of DL-Glyceraldehyde Reductase Activity in Rabbit Lens

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Abstract
Multiplicity of DL-glyceraldehyde reductase activity in rabbit lens was investigated. Enzymes with DL-glyceraldehyde reductase activity were separated into 2 fractions (F-1: unadsorbed enzyme fraction and F-2: adsorbed enzyme fraction) by dye-affinity chromatography using Matrex gel orange A. The fraction of F-2 was further separated into 4 fractions with DL-glyceraldehyde reductase activity (F-2a, F-2b, F-2c and F-2d) by chromatofocusing. The enzyme in F-1 was distinct from enzymes in F-2. The MW of the former was about 60,000, and that of the latter was about 33,000. The enzyme in F-1 was strongly active with D-erythrose as a substrate, and the enzymes in F-2 were strongly active with DL-glyceraldehyde. The enzyme in F-1 was not appreciably inhibited by aldose reductase inhibitors such as quercitrin, quercetin and 3,3-tetramethyleneglutaric acid, whereas the enzymes in F-2 were inhibited considerably. Sulfate ion did not activate the enzyme in F-1. Four enzymes in F-2 were subdivided into 2 groups (group A: F-2a and F-2c, group B: F-2b and F-2d) on the basis of their enzymatic properties. The enzymes in both groups A and B were capable of reducing various aldoses, but D-pentose and D-hexose were poor substrates for enzymes of group B. The enzymes in group A were activated by sulfate ion, and the enzymes in group B were not activated. The enzymes in group A were more susceptible to inhibition by aldose reductase inhibitors than those in group B.

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