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. 1990 Jun 15;268(3):529–537. doi: 10.1042/bj2680529

A comparative study of the N-linked oligosaccharide structures of human IgG subclass proteins.

R Jefferis 1, J Lund 1, H Mizutani 1, H Nakagawa 1, Y Kawazoe 1, Y Arata 1, N Takahashi 1
PMCID: PMC1131471  PMID: 2363690

Abstract

Quantitative oligosaccharide profiles were determined for each of 18 human IgG paraproteins representing the four subclasses. Each paraprotein exhibits a unique profile that may be substantially different from that observed for polyclonal IgG. The IgG2 and some IgG3 proteins analysed exhibit a predominance of oligosaccharide moieties having galactose on the Man(alpha 1----3) arm rather than the Man(alpha 1----6) arm; it was previously held that galactosylation of the Man(alpha 1----6) arm is preferred, as observed for IgG1, IgG4 and polyclonal IgG. An IgG4 protein is reported that has galactosylated Man(alpha 1----3) and Man(alpha 1----6) arms on both Fc-localized carbohydrate moieties; previous findings suggested that such fully glycosylated structures could not be accommodated within the internal space of the C gamma 2 domains. Unusual monoantennary oligosaccharides present in IgG2 and IgG3 proteins were isolated and their structures determined.

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Selected References

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