A Review of the Biological Significance of Carbohydrates on Glycoproteins and Methods for their Analysis
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.
KeywordsSialic Acid Glycan Structure Neuraminic Acid Glycan Site Primary Sequence Analysis
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- 8.Oxford GlycoSystems, Technical Bulletin No. 7, 1991Google Scholar
- 11.Kobata, A,. Biology of Carbohydrates, Wiley, 1984, 2, pp 87Google Scholar
- 13.Takeuchi, PNAS, 1986, pp 7819.Google Scholar
- 15.Gribben, The Lancet, 1990, pp 434 to 437.Google Scholar
- 19.Carlsson, D. M., J. Biol. Chem., 1968, 243, 616Google Scholar
- 21.Likhosherstov, L. M., Carbohydr. Res., 1988, 57, 785Google Scholar
- 24.Oxford GlycoSystems, GlycoPrep Update No. 1, 1991Google Scholar
- 29.Prime, S., et al., OGS Application Note IAN-01, 1993Google Scholar
- 30.Dearnley, J., et al., OGS poster titled ‘The RAAM Enzyme Array for Sialylated N-Glycans’, 1994Google Scholar