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.
Dates
Type | When |
---|---|
Created | 10 years ago (Aug. 10, 2015, 5:16 p.m.) |
Deposited | 3 years, 9 months ago (Nov. 25, 2021, 1:37 p.m.) |
Indexed | 3 weeks, 6 days ago (Aug. 7, 2025, 5:02 a.m.) |
Issued | 35 years, 2 months ago (June 15, 1990) |
Published | 35 years, 2 months ago (June 15, 1990) |
Published Print | 35 years, 2 months ago (June 15, 1990) |
@article{Jefferis_1990, title={A comparative study of the N-linked oligosaccharide structures of human IgG subclass proteins}, volume={268}, ISSN={1470-8728}, url={http://dx.doi.org/10.1042/bj2680529}, DOI={10.1042/bj2680529}, number={3}, journal={Biochemical Journal}, publisher={Portland Press Ltd.}, author={Jefferis, R and Lund, J and Mizutani, H and Nakagawa, H and Kawazoe, Y and Arata, Y and Takahashi, N}, year={1990}, month=jun, pages={529–537} }