[Physico-chemical characteristics of sorbitol dehydrogenase from the cytoplasm of bovine liver cells].
Partially purified preparation of sorbitol dehydrogenase, isolated from hepatocytes of bovine liver tissue, was active at a wide range of pH exhibiting the maximal activity at pH 9.0 in presence of NAD but not of NADP. The high rate of sorbitol and xylitol dehydration was observed, whereas the enzyme dehydrated ribitol at the 4-fold lower rate. Disc electrophoresis of the preparation in polyacrylamide gel, where sorbitol, xylitol and ribitol were used as substrates for colorimetric detection of the enzyme activity, exhibited six enzymatic zones with Rf 0.387, 0.266, 0.338, 0.193, 0.129 and 0.064. Optimal conditions were developed for storage of the active enzyme.
D000818:Animals; D002384:Catalysis; D002417:Cattle; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003593:Cytoplasm / Q000201:enzymology; D007700:Kinetics; D007064:L-Iditol 2-Dehydrogenase / Q000032:analysis*; D008099:Liver / Q000201:enzymology*; D013045:Species Specificity; D013379:Substrate Specificity; D013401:Sugar Alcohol Dehydrogenases / Q000032:analysis*
D013401:Sugar Alcohol Dehydrogenases; D007064:L-Iditol 2-Dehydrogenase
Fiziko-khimicheskie kharakteristiki sorbitoldegidrogenazy iz tsitoplazmy kletok pecheni byka.