Enzymatic hydrolysis of disaccharide unit of collagen. Isolation of 2-O-alpha-D-glucopyranosyl-O-beta-D-galactopyranosyl-hydroxylysine glucohydrolase from rat spleens

Eur J Biochem. 1980 Oct;111(2):587-91. doi: 10.1111/j.1432-1033.1980.tb04975.x.


The hydroxylsine-linked disaccharide unit, 2-O-alpha-D-glucopyranosyl-O-beta-D-galactopyranosyl-hydroxylysine (Glc-Gal-Hyl), prepared from collagens, was hydrolyzed by a glucohydrolase present in rat spleens and lungs. This disaccharide unit was scarcely hydrolyzed by homogenates of intestines, livers, and kidneys, which had a high alpha-D-glucosidase activity for neutral glucosides. The Glc-Gal-Hyl glucohydrolase was purified from rat spleens by affinity chromatography and gel filtration to the extent that sodium dodecyl sulfate/polyacrylamide gel electrophoresis gave a single band stained by Coomassie blue G-250. This purified glucohydrolase had a pH optimum around 5.8, and the Michaelis constant was 5.9 mM when Glc-Gal-Hyl was used as a substrate. This enzyme did not hydrolyze neutral glucosides. It is concluded that this Glc-Gal-Hyl glucohydrolase is responsible for catabolism of the hydroxylsine-linked disaccharide unit derived from collagens in mammals.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cations, Divalent
  • Collagen*
  • Disaccharides / analysis*
  • Glucosidases / metabolism*
  • Kinetics
  • Male
  • Rats
  • Spleen / enzymology*
  • Substrate Specificity
  • Tissue Distribution


  • Cations, Divalent
  • Disaccharides
  • Collagen
  • 2-O-alpha-D-glucopyranosyl-O-beta-D-galactopyranosyl-hydroxylysine glucohydrolase
  • Glucosidases