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Updated: May 18, 2026

Immunoglobulin G N-Glycan Analysis by Ultra-Performance Liquid Chromatography
Published on: January 18, 2020
CE analysis of γ-globulin mobility and potential clinical utility
Dieter Vanderschaeghe1, Evi Debruyne, Hans Van Vlierberghe
1Department for Molecular Biomedical Research, Unit for Molecular Glycobiology, VIB, Ghent, Belgium.
Abstract:
Serum protein electrophoresis is widely used in clinical laboratories to measure the relative abundance of each obtained fraction. Moreover, we found that the migration time of the γ-globulin fraction can be reproducibly determined (CV = 1.1%). Immunoglobulins were purified from serum using protein L-agarose and their N-glycosylation was studied using CE on a DNA sequencer. Liver fibrosis patients showed a lower level of sialylation and this moderately correlates with the migration time of the γ-globulins (r = 0.2-0.4). This allowed us to differentiate healthy individuals from these patients with an acceptable diagnostic accuracy (area under the curve = 0.75). This glycomics approach could become a significant added value to a daily, routine clinical test.
