Purification and properties of sorbitol dehydrogenase from mouse liver

Int J Biochem. 1983;15(4):507-11. doi: 10.1016/0020-711x(83)90124-6.

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Humans
  • Kinetics
  • L-Iditol 2-Dehydrogenase / isolation & purification*
  • L-Iditol 2-Dehydrogenase / metabolism
  • Liver / enzymology*
  • Macromolecular Substances
  • Mice
  • Mice, Inbred Strains
  • Molecular Weight
  • Species Specificity
  • Sugar Alcohol Dehydrogenases / isolation & purification*

Substances

  • Macromolecular Substances
  • Sugar Alcohol Dehydrogenases
  • L-Iditol 2-Dehydrogenase