Abstract
Three NADPH-linked aldehyde reductases (F 1, F 2 and F 3) could be separated by DEAE-cellulose chromatography from rabbit liver cytosol. These enzymes could be distinguished in regard to molecular weight, mobility in polyacrylamide gel electrophoresis, pH optima, substrate specificity and inhibitor sensitivity. Molecular weights of 33,000, 29,000 and 32.000 were estimated for F 1, F 2 and F 3, respectively, by gel filtration on Sephadex G-100. The F 2 was identical to aldehyde reductase (EC 1.1.1.2) from the substrate specificity for aromatic aldehydes and D-glucuronate and inhibition by barbiturates. The F 1 and F 3 were reductases for aromatic aldehydes and ketones, and had a higher affinity for aromatic ketones than for aromatic aldehydes, and were inhibited by sufhydryl reagents but not by barbiturates.
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