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Related Experiment Video

Updated: Jun 25, 2026

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases

Published on: December 26, 2011

IgG glycosylation analysis.

Carolin Huhn¹, Maurice H J Selman, L Renee Ruhaak

¹Biomolecular Mass Spectrometry Unit, Department of Parasitology, Leiden University Medical Center, Leiden, The Netherlands.

|February 13, 2009

Summary

This summary is machine-generated.

Monoclonal antibody (IgG) activity is influenced by N-glycans on the fragment crystallizable (Fc) region. Analyzing IgG glycosylation is crucial for understanding antibody function and developing new therapeutics.

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Last Updated: Jun 25, 2026

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases

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Mass Spectrometric Analysis of Glycosphingolipid Antigens

Mass Spectrometric Analysis of Glycosphingolipid Antigens

Published on: April 16, 2013

Area of Science:

Biochemistry
Immunology
Analytical Chemistry

Background:

Monoclonal IgG antibodies are key biotherapeutics.
N-glycans on the Fc region significantly modulate IgG biological activity.
Fc glycosylation impacts antibody-mediated cellular cytotoxicity and immunosuppressive properties.

Purpose of the Study:

To review and evaluate methods for IgG glycosylation analysis.
To highlight the importance of Fc glycosylation in therapeutic antibody function.
To discuss implications for understanding IgG in disease settings.

Main Methods:

Enzymatic or chemical release of N-glycans followed by chromatography or mass spectrometry.
Endoproteinase treatment (e.g., trypsin) for glycopeptide analysis via HPLC with ESI-MS.
Analysis of intact IgGs or fragments using MS, chromatography, or capillary electrophoresis (CE).

Main Results:

Different analytical approaches exist for comprehensive IgG glycosylation profiling.
Specific glycan structures (e.g., core-fucose absence, sialylation) have defined functional consequences.
Fc glycosylation analysis is essential for characterizing therapeutic antibodies and understanding disease-related changes.

Conclusions:

Accurate IgG glycosylation analysis is vital for biopharmaceutical development and quality control.
Understanding Fc glycosylation patterns provides insights into antibody efficacy and immunogenicity.
Advanced analytical techniques enable detailed characterization of IgG glycostructures.