title: Endoglycosidase and glycoamidase release of N-linked oligosaccharides.
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 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.
authors.affiliation: The Burnham Institute, La Jolla, California, USA.
authors.forename: Hudson H
authors.initials: HH
authors.lastname: Freeze
authors.forename: Christian
authors.initials: C
authors.lastname: Kranz
mesh_terms: D000581:Amidohydrolases / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D006026:Glycoside Hydrolases / Q000737:chemistry*; D006868:Hydrolysis; D009844:Oligosaccharides / Q000737:chemistry*
chemical_list: D009844:Oligosaccharides; D006026:Glycoside Hydrolases; D000581:Amidohydrolases