Tryptophan modification by 2-hydroxy-5-nitrobenzyl bromide studied by MALDI-TOF mass spectrometry

被引：10

作者：

Strohalm, M

Kodícek, M ^{[1
]}

Pechar, M

机构：

[1] Inst Chem Technol, Dept Biochem & Microbiol, CR-16628 Prague 6, Czech Republic

[2] Acad Sci Czech Republ, Inst Macromol Chem, Prague 16206 6, Czech Republic

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2003年 / 312卷 / 03期

关键词：

MALDI-TOF mass spectrometry; 2-hydroxy-5-nitrobenzyl bromide; Koshland reagent;

D O I：

10.1016/j.bbrc.2003.11.004

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The reaction with 2-hydroxy-5-nitrobenzyl bromide (HNB) is a common covalent modification of tryptophan. It results in several products which have been described by classical physico-chemical methods. To improve the understanding of the HNB-modified tryptophan structure, we synthesized a model peptide containing one tryptophan only, modified it by HNB, and analyzed the product by MALDI-TOF mass spectrometry. Surprisingly, several multi-modified products (up to 5 HNB moieties per one tryptophan) were identified. the influence of HNB concentration and pH on the degree of modification was also analyzed. In addition, a splitting of modified tryptophan peaks in MALDI-TOF spectrum was described; most probably, this effect is a common MALDI artifact of nitro-aromatic compounds which facilitates the identification of HNB-modified tryptophan by MALDI-TOF MS significantly. (C) 2003 Elsevier Inc. All rights reserved.

引用

页码：811 / 816

页数：6

共 16 条

[1] Active site characterization of the exo-N-acetyl-β-D-glucosaminidase from thermotolerant Bacillus sp NCIM 5120:: involvement of tryptophan, histidine and carboxylate residues in catalytic activity [J].