Comparison of the Fc glycosylation of fetal and maternal immunoglobulin G

Human immunoglobulin G (IgG) molecules are composed of two Fab portions and one Fc portion. The glycans attached to the Fc portions of IgG are known to modulate its biological activity as they influence interaction with both complement and various cellular Fc receptors. IgG glycosylation changes sig...

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Veröffentlicht in:	Glycoconjugate journal 2013-02, Vol.30 (2), p.147-157
Hauptverfasser:	Einarsdottir, Helga K., Selman, Maurice H. J., Kapur, Rick, Scherjon, Sicco, Koeleman, Carolien A. M., Deelder, André M., van der Schoot, C. Ellen, Vidarsson, Gestur, Wuhrer, Manfred
Format:	Artikel
Sprache:	eng
Schlagworte:	Biochemistry Biomedical and Life Sciences Chromatography, Liquid Female Glycoproteins Glycosylation Humans Immunoglobulin G - chemistry Immunoglobulin G - metabolism Immunoglobulins Infant, Newborn Life Sciences Mass Spectrometry Pathology Peptides Pregnancy Receptors, Fc - chemistry Receptors, Fc - metabolism
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