A method for terminus proteomics: Selective isolation and labeling of N-terminal peptide from protein through transamination reaction

被引：10
作者：
Sonomura, Kazuhiro [1 ,2 ]
Kuyama, Hiroki [1 ]
Matsuo, Ei-ichi [1 ,2 ]
Tsunasawa, Susumu [1 ]
Nishimura, Osamu [1 ]
机构：
[1] Osaka Univ, Inst Prot Res, Suita, Osaka 5650871, Japan
[2] Shimadzu Co Ltd, Technol Res Lab, Life Sci Res Ctr, Kyoto 6190237, Japan
来源：
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 2009年 / 19卷 / 23期
关键词：
Transamination; N-terminal labeling; MALDI-TOF MS; N-terminal sequence analysis; DESORPTION/IONIZATION MASS-SPECTROMETRY; SEQUENCE-ANALYSIS; GRIFOLA-FRONDOSA; EXTRA METHIONINE; FRUITING BODIES; MATRIX; METALLOENDOPEPTIDASE; CLEAVAGE; ACIDS; TIME;
D O I：
10.1016/j.bmcl.2009.10.044
中图分类号：
R914 [药物化学];
学科分类号：
100701 ;
摘要：
A novel method for selectively labeling and isolating N-terminal peptide from protein has been developed. An N-alpha-amino group of protein was converted to a carbonyl group through transamination reaction and the resulting carbonyl group was modified with O-(4-nitrobenzyl)hydroxylamine (NBHA). After proteolytic digestion using Grifola frondosa metalloendopeptidase (LysN), the modified N-terminal peptide remained unbound in the following treatment using amino-reactive p-phenylenediisothiocyanate (DITC) glass, whereas peptides other than the N-terminal peptide were effectively scavenged from the supernatant solution. The modified N-terminal peptide was thus successfully isolated and sequenced by matrix-assisted laser desorption/ionization tandem mass spectrometry (MALDI-MS/MS) analysis. (C) 2009 Elsevier Ltd. All rights reserved.
引用
收藏
页码：6544 / 6547
页数：4
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