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首页> 外文期刊>Journal of mass spectrometry: JMS >MALDI mass spectrometry-based sequence analysis of arginine-containing glycopeptides: Improved fragmentation of glycan and peptide chains by modifying arginine residue
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MALDI mass spectrometry-based sequence analysis of arginine-containing glycopeptides: Improved fragmentation of glycan and peptide chains by modifying arginine residue

机译：基于MALDI质谱的含精氨酸糖肽序列分析：通过修饰精氨酸残基改善聚糖和肽链的断裂

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摘要

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 α_1-acid glycoprotein-derived N-linked glycopeptides, and glycan and peptide in each glycopeptide were successfully sequenced by MALDI tandem MS (MS/MS).
机译：本文介绍了一种通过MALDI质谱（MS）进行含Arg糖肽序列分析的改进方法。该方法使用氨基衍生化（4-氮杂-6-（2,6-二甲基-1-哌啶基）-5-氧代己酸N-琥珀酰亚胺酯）并去除（羧肽酶B）或修饰（肽基精氨酸脱亚氨酶4）肽的残基。衍生作用将碱性叔胺部分连接到肽上，酶处理可去除或修饰精氨酸残基。在低能碰撞诱导的解离下，所得糖肽的片段化产生了聚糖和肽的简化离子序列，可以促进它们的测序。用α_1-酸糖蛋白衍生的N-连接糖肽研究了该方法的可行性，并通过MALDI串联质谱（MS / MS）成功地测序了每个糖肽中的聚糖和肽。

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