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Mol Cell Proteomics. 2013 Apr;12(4):856-65. doi: 10.1074/mcp.R112.026005. Epub 2013 Jan 16.

Glycoproteomic analysis of antibodies.

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  • 1Biomolecular Mass Spectrometry Unit, Postbus 9600, 2300RC Leiden University Medical Center, Leiden, The Netherlands.

Abstract

Antibody glycosylation has been shown to change with various processes. This review presents mass spectrometric approaches for antibody glycosylation analysis at the level of released glycans, glycopeptides, and intact protein. With regard to IgG fragment crystallizable glycosylation, mass spectrometry has shown its potential for subclass-specific, high-throughput analysis. In contrast, because of the vast heterogeneity of peptide moieties, fragment antigen binding glycosylation analysis of polyclonal IgG relies entirely on glycan release. Next to IgG, IgA has gained some attention, and studies of its O- and N-glycosylation have revealed disease-associated glycosylation changes. Glycoproteomic analyses of IgM and IgE are lagging behind but should complete our picture of glycosylation's influence on antibody function.

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