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Enhancing the intensities of lysine‐terminated tryptic peptide ions in matrix‐assisted laser desorption/ionization mass spectrometry
Author(s) -
Beardsley Richard L.,
Karty Jonathan A.,
Reilly James P.
Publication year - 2000
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/1097-0231(20001215)14:23<2147::aid-rcm145>3.0.co;2-m
Subject(s) - chemistry , lysine , mass spectrometry , matrix assisted laser desorption/ionization , peptide , protein mass spectrometry , desorption , chromatography , sample preparation in mass spectrometry , ion , matrix (chemical analysis) , analytical chemistry (journal) , tandem mass spectrometry , biochemistry , amino acid , electrospray ionization , organic chemistry , adsorption
Tryptic digests of three proteins are reacted with O ‐methylisourea in order to convert lysine residues to homoarginines. The resulting homoarginine‐terminated peptides exhibit more intense MALDI mass spectral peaks than their lysine‐terminated predecessors. This simple chemical reaction should therefore facilitate protein sequencing and mass mapping. Copyright © 2000 John Wiley & Sons, Ltd.