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.
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Dennis, R.P. (1995). A Review of the Biological Significance of Carbohydrates on Glycoproteins and Methods for their Analysis. In: Alavi, A., Axford, J.S. (eds) Glycoimmunology. Advances in Experimental Medicine and Biology, vol 376. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1885-3_1
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DOI: https://doi.org/10.1007/978-1-4615-1885-3_1
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