Unit

UNIT 17.13A Endoglycosidase and Glycoamidase Release of N-Linked Glycans

  1. Hudson H. Freeze,
  2. Christian Kranz

Published Online: 1 JAN 2010

DOI: 10.1002/0471142727.mb1713as89

Current Protocols in Molecular Biology

Current Protocols in Molecular Biology

How to Cite

Freeze, H. H. and Kranz, C. 2010. Endoglycosidase and Glycoamidase Release of N-Linked Glycans. Current Protocols in Molecular Biology. 89:III:17.13A:17.13A.1–17.13A.25.

Author Information

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

Publication History

  1. Published Online: 1 JAN 2010
  2. Published Print: JAN 2010

Abstract

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 trafficks from the ER to the Golgi toward its final location. Curr. Protoc. Mol. Biol. 89:17.13A.1-17.13A.25. © 2010 by John Wiley & Sons, Inc.

Keywords:

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