Membrane-bound sorbitol dehydrogenase in human red blood cells. Studies in normal subjects and in enzyme-deficient subjects with congenital cataracts

J Inherit Metab Dis. 1993;16(1):67-72. doi: 10.1007/BF00711317.

Abstract

Membrane-bound and soluble forms of erythrocyte sorbitol dehydrogenase (SORD) activity are compared in normal individuals. Both isoenzymes showed similar properties. In a family with red cell SORD deficiency and congenital cataracts, Km values for sorbitol and NAD+ as well as the effect of the enzymatic deficiency on sorbitol accumulation in red cells incubated in high-glucose or high-fructose media were determined. In SORD-deficient patients, the enzymatic deficiency was observed in both crude haemolysate and SORD-M preparations with sorbitol, galactitol, xylitol or ribitol as substrates. The mutation responsible for SORD deficiency did not modify the Km for sorbitol and NAD+. Finally, SORD deficiency produced a significant increase of sorbitol accumulation in red cells incubated in high-concentration glucose media and a significant decrease when the cells were incubated in high-concentration fructose media.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cataract / congenital*
  • Cataract / enzymology
  • Cataract / genetics
  • Erythrocyte Membrane / enzymology*
  • Female
  • Humans
  • Isoenzymes / blood
  • Kinetics
  • L-Iditol 2-Dehydrogenase / blood*
  • L-Iditol 2-Dehydrogenase / deficiency
  • Male
  • Pedigree
  • Phenotype
  • Sorbitol / blood
  • Spectrometry, Fluorescence
  • Spectrophotometry, Ultraviolet
  • Substrate Specificity

Substances

  • Isoenzymes
  • Sorbitol
  • L-Iditol 2-Dehydrogenase