Comparison of separation techniques for the elucidation of IgG N-glycans pooled from healthy mammalian species October 24, 2014 Adamczyk B1, Tharmalingam-Jaikaran T2, Schomberg M2, Szekrényes Á3, Kelly RM2, Karlsson NG4, Guttman A5, Rudd PM6. Carbohydr Res. 2014 May 7;389:174-85. Show Affiliations 1GlycoScience Group, NIBRT-The National Institute for Bioprocessing Research and Training, Fosters Avenue, Mount Merrion, Blackrock, Co. Dublin, Ireland; Medical Biochemistry, University of Gothenburg, Gothenburg, Sweden and 2GlycoScience Group, NIBRT-The National Institute for Bioprocessing Research and Training, Fosters Avenue, Mount Merrion, Blackrock, Co. Dublin, Ireland and 3Horváth Laboratory for Bioseparation Sciences, Research Center for Molecular Medicine, University of Debrecen, 4032 Debrecen, Hungary and 4Medical Biochemistry, University of Gothenburg, Gothenburg, Sweden and 5Horváth Laboratory for Bioseparation Sciences, Research Center for Molecular Medicine, University of Debrecen, 4032 Debrecen, Hungary; MTA-TKI Translational Glycomics Research Group, University of Pannonia, Veszprem, Hungary and 6GlycoScience Group, NIBRT-The National Institute for Bioprocessing Research and Training, Fosters Avenue, Mount Merrion, Blackrock, Co. Dublin, Ireland. Electronic address: [email protected] 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. Copyright © 2014 Elsevier Ltd. All rights reserved. Go To PubMed Figure Legend: Variability of N-glycosylation profiles of human, bovine, ovine, equine, canine and feline IgG using HILIC-FLD-UPLC. 2014-10-24 GMD staff
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