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Peptide sequencing through N‐terminal phosphonylation and electrospray ionization mass spectrometry
Author(s) -
Bao Jiangyin,
Ai Huiwang,
Fu Hua,
Jiang Yuyang,
Zhao Yufen,
Huang Cheng
Publication year - 2005
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/jms.850
Subject(s) - chemistry , electrospray ionization , mass spectrometry , protein mass spectrometry , peptide , tandem mass spectrometry , electrospray , chromatography , tandem mass tag , sample preparation in mass spectrometry , mass spectrum , triethylamine , isobaric labeling , peptide sequence , ion , organic chemistry , proteomics , biochemistry , quantitative proteomics , gene
Peptides were phosphonylated at their N‐termini by reacting with ethoxyphenylphosphinate in the presence of triethylamine and tetrachloromethane under mild conditions. The phosphonylated peptides were analyzed by tandem electrospray ionization mass spectrometry. N‐Terminal phosphonylation selectively increased the intensities of b n ‐type ions relative to other ion types. The resulting simplified mass spectra clearly show the sequential loss of amino acid residues from the C‐termini of peptides, providing a convenient and rapid method for peptide sequencing. Copyright © 2005 John Wiley & Sons, Ltd.