Antibody glycosylation has been shown to change with various processes. This review presents mass spectro-metric approaches for antibody glycosylation analysis at the level of released glycans, glycopeptides, and intact protein. With regard to IgG fragment crystallizable glyco-sylation, 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 poly-clonal 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.,
Molecular and Cellular Proteomics
This work was funded by the European Commission 7th Framework Programme; grant id fp7/278535 - Methods for high-throughput (HTP) analysis of protein glycosylation (HIGHGLYCAN)
Erasmus MC: University Medical Center Rotterdam

Zauner, G, Selman, M.H.J, Bondt, A, Rombouts, Y, Blank, D, Deelder, A.M, & Wuhrer, M. (2013). Glycoproteomic analysis of antibodies. Molecular and Cellular Proteomics (Vol. 12, pp. 856–865). doi:10.1074/mcp.R112.026005