UNIT 8.15 Endoglycosidase and Glycoamidase Release of N-Linked Glycans

  1. Hudson H. Freeze,
  2. Christian Kranz

Published Online: 1 NOV 2008

DOI: 10.1002/0471142735.im0815s83

Current Protocols in Immunology

Current Protocols in Immunology

How to Cite

Freeze, H. H. and Kranz, C. 2008. Endoglycosidase and Glycoamidase Release of N-Linked Glycans. Current Protocols in Immunology. 83:IV:8.15:8.15.1–8.15.26.

Author Information

  1. Burnham Institute for Medical Research, La Jolla, California

Publication History

  1. Published Online: 1 NOV 2008
  2. Published Print: NOV 2008

This is not the most recent version of the article. View current version (1 APR 2010)


Nearly all proteins entering the lumen of the endoplasmic reticulum (ER) become glycosylated en route to a cellular organelle, the plasma membrane, or the extracellular space. Many glycans can be attached to proteins, but the most common are the N-linked glycans (oligosaccharides). These chains are added very soon after a protein enters the ER, but they undergo extensive remodeling (processing), especially in the Golgi. Processing changes the sensitivity of the N-glycan to enzymes that cleave entire sugar chains or individual monosaccharides, which also changes the migration of the protein on SDS gels. These changes can be used to indicate when a protein has passed a particular subcellular location. This unit details some of the methods used to track a protein as it traffics from the ER to the Golgi toward its final location. Curr. Protoc. Immunol. 83:8.15.1-8.15.26. © 2008 by John Wiley & Sons, Inc.


  • ER/Golgi;
  • oligosaccharide;
  • glycan;
  • N-glycosylation;
  • glycosidase;
  • intracellular trafficking