Purification and characterization of the multiple forms of aldehyde reductase in ox kidney

Abstract

Aldehyde reductase from ox kidney cytosol was fractionated into 4 forms, 2 of which were purified to apparent homogeneity. One of the minor forms is heterogenous on polyacrylamide-gel electrophoresis. The substrate specificities of the 4 forms using a variety of aldehydes and ketones are presented. The sensitivity of the various forms to inhibition by sodium valproate, sodium barbitone and various benzodiazepines was determined. The relationships of these forms to the previously described hexonate dehydrogenase, aldose reductase and prostaglandin dehydrogenase is discussed.