The role of oligosaccharides in modifying protein function

Ciba Found Symp. 1989;145:241-55; discussion 255-6. doi: 10.1002/9780470513828.ch14.


It has been proposed that protein-bound oligosaccharides interact with the protein to which they are attached to up- or down-regulate the bioactivity of the 'composite' glycoprotein. Oligosaccharide analyses of the glycoproteins Thy-1, tissue plasminogen activator and immunoglobulin G are presented. Correlations between particular glycoforms and enzymic activities are demonstrated for tissue plasminogen activator. The change in the prevalence of particular immunoglobulin G glycoforms is shown to correlate with disease activity in rheumatoid activity.

Publication types

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

MeSH terms

  • Animals
  • Antigens, Surface
  • Arthritis, Rheumatoid / immunology
  • Glycoproteins / physiology*
  • Humans
  • Immunoglobulin G / physiology
  • Membrane Glycoproteins / physiology
  • Models, Molecular
  • Oligosaccharides / physiology*
  • Protein Conformation
  • Thy-1 Antigens
  • Tissue Plasminogen Activator / physiology


  • Antigens, Surface
  • Glycoproteins
  • Immunoglobulin G
  • Membrane Glycoproteins
  • Oligosaccharides
  • Thy-1 Antigens
  • Tissue Plasminogen Activator