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

Autor:	Kenichi, Taniguchi, Hiroki, Kuyama, Shigeki, Kajihara, Koichi, Tanaka
Rok vydání:	2013
Předmět:	Models Chemical Polysaccharides Sequence Analysis Protein Tandem Mass Spectrometry Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Molecular Sequence Data Glycopeptides Citrulline Humans Amino Acid Sequence Arginine
Zdroj:	Journal of mass spectrometry : JMS. 48(8)
ISSN:	1096-9888
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).
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::5d7761d784935eb1b771776496241f54 https://pubmed.ncbi.nlm.nih.gov/23893643 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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