Differentiation between isomeric triantennaryN-linked glycans by negative ion tandem mass spectrometry and confirmation of glycans containing galactose attached to the bisecting (β1-4-GlcNAc) residue inN-glycans from IgG

4-substituted on the core mannose) residue recently reported by Takegawa et al. from N-glycans released from human immunoglobulin G (IgG). We extend this analysis of human serum IgG to reveal an analogue of the fucosylated triantennary glycan reported by Takegawa et al. together with a third compound that lacked both the sialic acid and the fucose residues. In addition, we demonstrate the biosynthesis of bisected hybrid-type glycans with the galactose modification, with and without core fucose, on the stem cell marker glycoprotein, 19A, expressed in a partially ricin-resistant human embryonic kidney cell line. It would appear, therefore, that this modification of N-linked glycans containing a galactosylated bisecting GlcNAc residue may be more common than originally thought. Negative ion MS/MS analysis of glycans is likely to prove an invaluable tool in the analysis and monitoring of therapeutic glycoproteins. -->

ISSN:	1097-0231 0951-4198
DOI:	10.1002/rcm.3470
Přístupová URL adresa:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::427faed53dc684b4c020a394bb7228a6 https://doi.org/10.1002/rcm.3470
Rights:	CLOSED
Přírůstkové číslo:	edsair.doi.dedup.....427faed53dc684b4c020a394bb7228a6
Autor:	Christopher N. Scanlan, Pauline M. Rudd, Max Crispin, Bernhard B. Singer, Veronica T. Chang, Smita Thobhani, Catherine M. Radcliffe, Chun Ting Yuen, Lothar Lucka, David Harvey
Rok vydání:	2008
Předmět:	Anions Spectrometry Mass Electrospray Ionization Glycan Mannose Tandem mass spectrometry Sensitivity and Specificity Fucose Analytical Chemistry chemistry.chemical_compound Residue (chemistry) Isomerism Polysaccharides Biomarkers Tumor Spectroscopy chemistry.chemical_classification biology Organic Chemistry Galactose Reproducibility of Results Sialic acid carbohydrates (lipids) chemistry Biochemistry Immunoglobulin G Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization biology.protein N-Acetylgalactosaminyltransferases Glycoprotein Oligopeptides
Zdroj:	Rapid Communications in Mass Spectrometry. 22:1047-1052
ISSN:	1097-0231 0951-4198
DOI:	10.1002/rcm.3470
Popis:	Negative ion tandem mass spectrometry (MS/MS) spectra of three isomeric triantennary N-linked glycans provided clear differentiation between the isomers and confirmed the occurrence of an isomer that was substituted with galactose on a bisecting GlcNAc (1 --> 4-substituted on the core mannose) residue recently reported by Takegawa et al. from N-glycans released from human immunoglobulin G (IgG). We extend this analysis of human serum IgG to reveal an analogue of the fucosylated triantennary glycan reported by Takegawa et al. together with a third compound that lacked both the sialic acid and the fucose residues. In addition, we demonstrate the biosynthesis of bisected hybrid-type glycans with the galactose modification, with and without core fucose, on the stem cell marker glycoprotein, 19A, expressed in a partially ricin-resistant human embryonic kidney cell line. It would appear, therefore, that this modification of N-linked glycans containing a galactosylated bisecting GlcNAc residue may be more common than originally thought. Negative ion MS/MS analysis of glycans is likely to prove an invaluable tool in the analysis and monitoring of therapeutic glycoproteins.
Databáze:	OpenAIRE
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