MALDI mass spectrometry-based sequence analysis of arginine-containing glycopeptides: improved fragmentation of glycan and peptide chains by modifying arginine residue

Autor:	Shigeki Kajihara, Taniguchi Kenichi, Koichi Tanaka, Hiroki Kuyama
Rok vydání:	2013
Předmět:	chemistry.chemical_classification Glycan Chromatography Arginine Tertiary amine biology Sequence analysis Peptide Mass spectrometry Glycopeptide chemistry.chemical_compound chemistry biology.protein Derivatization Spectroscopy
Zdroj:	Journal of Mass Spectrometry. 48:951-960
ISSN:	1076-5174
DOI:	10.1002/jms.3241
Popis:	This paper describes an improved method for the sequence analysis of Arg-containing glycopeptide by MALDI mass spectrometry (MS). The method uses amino group derivatization (4-aza-6-(2,6-dimethyl-1-piperidinyl)-5-oxohexanoic acid N-succinimidyl ester) and removal (carboxypeptidase B) or modification (peptidylarginine deiminase 4) of the arginine residue of the peptide. The derivatization attaches a basic tertiary amine moiety onto the peptides, and the enzymatic treatment removes or modifies the arginine residue. Fragmentation of the resulting glycopeptide under low-energy collision-induced dissociation yielded a simplified ion series of both the glycan and the peptide that can facilitate their sequencing. The feasibility of the method was studied using α1-acid glycoprotein-derived N-linked glycopeptides, and glycan and peptide in each glycopeptide were successfully sequenced by MALDI tandem MS (MS/MS). Copyright © 2013 John Wiley & Sons, Ltd.
Databáze:	OpenAIRE
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