期刊
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
卷 19, 期 23, 页码 6544-6547出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmcl.2009.10.044
关键词
Transamination; N-terminal labeling; MALDI-TOF MS; N-terminal sequence analysis
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.
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