A Review of the Biological Significance of Carbohydrates on Glycoproteins and Methods for their Analysis

  • Richard P. Dennis
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 376)

Abstract

Most secreted and cell surface proteins are glycosylated. There are three principal ways by which glycans may be attached to the protein: via the amino acid sequon of Asn-Xxx-Ser/Thr for N-glycosylation, the amino acids Ser/Thr for O-glycosylation and the C terminal amino acid in the GPI anchor of membrane bound glycoproteins. Typically a glycoprotein has greater than three glycan sites, each site containing between 10 and 30 structures. The presence of this many glycans on a single protein gives rise to the concept of glycoforms. Glycans on the protein can profoundly affect the 3-D structure of the protein and its biological function.1 The study of these glycans is therefore important whether one is involved in glycoprotein basic research, structure/function relationships, recombinant glycoprotein production or recombinant protein quality control.

Keywords

Sugar Fermentation Carbohydrate Half Life Anhydride 

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Copyright information

© Springer Science+Business Media New York 1995

Authors and Affiliations

  • Richard P. Dennis
    • 1
  1. 1.Unit 4, Hitching CourtOxford GlycoSystemsAbingdonUK

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