Enzymatic Release of O-and N-Linked Oligosaccharide Chains

  • Elizabeth F. Hounsell
  • Michael J. Davies
  • Kevin D. Smith
Part of the Springer Protocols Handbooks book series (SPH)


Enzymes involved in both the synthesis and degradation of glycoconjugates are highly specific for monosaccharide, linkage position, and anomeric configuration factors further away in the oligosaccharide sequence or protein. Not withstanding this, endo- and exoglycosidases are extremely useful tools in structural analysis. The RAAM technique has automated the use of exoglycosidase digestion (Oxford Glycosystems, Abingdon, UK). Here we discuss the release of intact oligosaccharide chains from proteins that can be further analyzed for separate functions (1,2).


Sialic Acid Potassium Dihydrogen Sialic Acid Residue Separate Function Digestion Buffer 
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  1. 1.
    Yamamoto, K., Tsuji, T., and Osawa, T. (1993) Analysis of asparagine-linked oligosaccharides by sequential lectin-affinity chromatography, in Methods in Molecular Biology, vol. 14: Glycoprotein Analysis in Biomedicine (Hounsell, E. F., ed.), Humana, Totowa, NJ, pp. 17–34.CrossRefGoogle Scholar
  2. 2.
    Davies, M. J., Smith, K. D., and Hounsell, E. F. (1994) The release of oligosaccharides from glycoproteins, in Methods in Molecular Biology, vol. 32: Basic Protein and Peptide Protocols (Walker, J. M., ed.), Humana, Totowa, NJ, pp. 129–141.CrossRefGoogle Scholar

Copyright information

© Humana Press Inc., Totowa, NJ 2002

Authors and Affiliations

  • Elizabeth F. Hounsell
    • 1
  • Michael J. Davies
  • Kevin D. Smith
  1. 1.School of Biological and Chemical SciencesBirkbeck University of LondonUK

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