title: Purification and properties of sorbitol dehydrogenase from mouse liver.
abstract: 1. The sorbitol dehydrogenase (L-iditol: NAD oxidoreductase, EC 1.1.1.14) from mouse liver has been purified to homogeneity. 2. The enzyme has a mol. wt of 140,000 and is composed of four identical subunits of mol. wt 35,000. 3. the purified enzyme catalyses both sorbitol oxidation and fructose reduction. 4. It is specific for NAD+ (NADH) and does not function with NADP+ (NADPH). 5. The Michaelis constants for sorbitol, fructose, NAD+ and NADPH are 1.54 and 154 mM, 58.8 and 15 microM, respectively. 6. The enzyme is SH-group reagent sensitive and is strongly inhibited by 1,10-phenanthroline.
mesh_terms: D000818:Animals; D006801:Humans; D007700:Kinetics; D007064:L-Iditol 2-Dehydrogenase / Q000302:isolation & purification* / Q000378:metabolism; D008099:Liver / Q000201:enzymology*; D046911:Macromolecular Substances; D051379:Mice; D008815:Mice, Inbred Strains; D008970:Molecular Weight; D013045:Species Specificity; D013401:Sugar Alcohol Dehydrogenases / Q000302:isolation & purification*
chemical_list: D046911:Macromolecular Substances; D013401:Sugar Alcohol Dehydrogenases; D007064:L-Iditol 2-Dehydrogenase