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- W145582461 abstract "The IgG antibody molecule is a structural paradigm for members of the immuoglobulin super family1. Whilst the oligosaccharide moiety of the IgG molecule accounts for only 23% of its mass it has been shown to be essential for optimal activation of effector mechanisms leading to the clearance and destruction of pathogens2, 3, 4. Human antibody molecules of the IgG class have N-linked oligosaccharide attached at the amide side chain of Asn-297 in the heavy chain5. The oligosaccharide moiety is of the complex bianntennary type having a heptasaccharide “core” structure (GlcNAc2Man3GlcNAc2) and variable outer arm “non-core” sugar residues, such as fucose, bisecting N-acetylglucosamine, galactose and sialic acid (Figure 1). The number of variant oligosaccharides that may be attached to heavy chains is 32 (Figure 2) and the total number of possible glycoforms >8006,7. This level of heterogeneity is evident for polyclonal IgG whilst a more restricted heterogeneity may be observed for monoclonal proteins4. In addition, ~30% of polyclonal IgG has been reported to bear a complex N- linked oligosaccharide in the Fab region8. It is apparent, therefore, that glycosylation is a post-translational modification that can introduce a very significant structural and, possibly, functional heterogeneity into the IgG molecule, such that glycoforms can alter the biological activity9." @default.
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- W145582461 date "1998-01-01" @default.
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- W145582461 title "A Longitudinal Study of Glycosylation of a Human IgG3 Paraprotein in a Patient with Multiple Myeloma" @default.
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- W145582461 doi "https://doi.org/10.1007/978-1-4615-5383-0_10" @default.
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