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Article

Hinge-Region O-Glycosylation of Human Immunoglobulin G3 (IgG3).

Molecular & cellular proteomics : MCP - 1 May 2015

Plomp Rosina, Dekkers Gillian, Rombouts Yoann, Visser Remco, Koeleman Carolien A M, Kammeijer Guinevere S M, Jansen Bas C, Rispens Theo, Hensbergen Paul J, Vidarsson Gestur, Wuhrer Manfred

Abstract excerpt

Immunoglobulin G (IgG) is one of the most abundant proteins present in human serum and a fundamental component of the immune system. IgG3 represents ∼8% of the total amount of IgG in human serum and stands out from the other IgG subclasses because of its elongated hinge region and enhanced effector functions. This study reports partial O-glycosylation of the IgG3 hinge region, observed with nanoLC-ESI-IT-MS(/MS)...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 25759508
DOI: 10.1074/mcp.M114.047381
PMCID: PMC4424406

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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