title: Polyol dehydrogenase: purification. Evidence for multiple forms and some properties of the dominant variant of the horse liver enzyme.
abstract: Purification of horse-liver polyol dehydrogenase (PDH) on DE52 anion-exchange cellulose reveals the presence of three fractions with enzyme activity. These appear in the breakthrough volume (PDH-3) and the salt gradient (PDH-1, -2) respectively. The major band of activity (greater than approximately 90%) is found in the PDH-2 fraction. A reexamination of sheep-liver polyol dehydrogenase also reveals the presence of three bands of activity, with the dominant fraction (PDH-3) corresponding to the preparation described by Smith (Biochem. J., 83, 135-144, (1962)). The interaction between horse-liver (and sheep-liver) PDH and Blue Sepharose CL-6B is found to be endothermic. This property is utilized in the final purification step. Horse-liver PDH-2 has a molecular/subunit weight of approximately 85,000/approximately 28,000, a Stokes' radius of 3.8 nm, and an isoelectric point of 7.4.
mesh_terms: D000449:Aldehyde Reductase; D000818:Animals; D002846:Chromatography, Affinity / Q000379:methods; D002848:Chromatography, DEAE-Cellulose / Q000379:methods; D002850:Chromatography, Gel / Q000379:methods; D006736:Horses; D007527:Isoenzymes / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D013379:Substrate Specificity; D013401:Sugar Alcohol Dehydrogenases / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: D007527:Isoenzymes; D013401:Sugar Alcohol Dehydrogenases; D000449:Aldehyde Reductase; C023142:polyol dehydrogenase (NADP)