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. 2010 Apr:Chapter 8:8.15.1-8.15.25.
doi: 10.1002/0471142735.im0815s89.

Endoglycosidase and glycoamidase release of N-linked glycans

Hudson H Freeze  1 , Christian Kranz  1
Affiliations

Endoglycosidase and glycoamidase release of N-linked glycans

Hudson H Freeze et al. Curr Protoc Immunol. 2010 Apr.

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.

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References

Literature Cited

References
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Key References
    1. Beckers et al., 1987. See above.
    1. Chui et al., 1997. See above.
    1. Kornfeld and Kornfeld, 1985. See above.
    1. Tarentino and Plummer, 1994. See above.

MeSH terms

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