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Comparison of separation techniques for the elucidation of IgG N-glycans pooled from healthy mammalian species

Journal article
Authors Barbara Adamczyk
Tharmala Tharmalingam-Jaikarana
Michael Schomberg
Ákos Szekrényes
Ronan M. Kelly
Niclas G. Karlsson
Andràs Guttman
Pauline M. Rudd
Published in Carbohydrate Research
Volume 389
Pages 174-185
ISSN 0008-6215
Publication year 2014
Published at Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 174-185
Language en
Links dx.doi.org/10.1016/j.carres.2014.01...
Keywords Protein glycosylation; IgG; Glycan analysis; HILIC–UPLC; RP–UPLC; CE-LIF
Subject categories Biomedical Laboratory Science/Technology

Abstract

The IgG N-glycome provides sufficient complexity and information content to serve as an excellent source for biomarker discovery in mammalian health. Since oligosaccharides play a significant role in many biological processes it is very important to understand their structure. The glycosylation is cell type specific as well as highly variable depending on the species producing the IgG. We evaluated the variation of N-linked glycosylation of human, bovine, ovine, equine, canine and feline IgG using three orthogonal glycan separation techniques: hydrophilic interaction liquid chromatography (HILIC)–UPLC, reversed phase (RP)–UPLC and capillary electrophoresis with laser induced fluorescence detection (CE-LIF). The separation of the glycans by these high resolution methods yielded different profiles due to diverse chemistries. However, the % abundance of structures obtained by CE-LIF and HILIC–UPLC were similar, whereas the analysis by RP-UPLC was difficult to compare as the structures were separated by classes of glycans (highly mannosylated, fucosylated, bisected, fucosylated and bisected) resulting in the co-elution of many structures. The IgGs from various species were selected due to the complexity and variation in their N-glycan composition thereby highlighting the complementarity of these separation techniques.

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