A model for cleavage of O-glycosidic bonds in glycoproteins.

Glycoconj J

Department of Molecular and Radiation Biophysics, Petersburg Nuclear Physics Institute, Gatchina, Russia.

Published: June 1993

AI Article Synopsis

  • The study explored how alpha-mannosidase and alpha-galactosidase enzymes can break the alpha-linkages between sugars (mannose or galactose) and amino acids (serine/threonine).
  • Initial experiments used synthetic models that mimic the O-glycosidic bonds found in glycoproteins.
  • The research concluded that these enzymes are capable of hydrolyzing the linkages after the glucoamylase undergoes proteolytic digestion.

Article Abstract

The present work investigated the possibility of cleavage of alpha-linkages between mannose or galactose and serine/threonine residues by alpha-mannosidase and alpha-galactosidase. The study was carried out initially with model synthetic compounds imitating the O-glycosidic bond in glycoproteins, and further with glucoamylase. It was shown that alpha-mannosidase and alpha-galactosidase can hydrolyse these linkages after proteolytic digestion of glucoamylase.

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http://dx.doi.org/10.1007/BF00702202DOI Listing

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