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Ion trap mass spectrometry in the structural analysis of haemoglobin peptides modified by epichlorohydrin and diepoxybutane
Author(s) -
Miraglia Nadia,
Basile Adriana,
Pieri Maria,
Acampora Antonio,
Malorni Livia,
Giulio Beatrice De,
Sannolo Nicola
Publication year - 2002
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/rcm.645
Subject(s) - chemistry , mass spectrometry , fragmentation (computing) , ion trap , quadrupole ion trap , mass spectrum , epichlorohydrin , top down proteomics , chromatography , protein mass spectrometry , sample preparation in mass spectrometry , ion , tandem mass spectrometry , analytical chemistry (journal) , organic chemistry , electrospray ionization , computer science , operating system
Ion trap mass spectrometry has been shown to be particularly suitable for the structural analysis of high molecular weight peptides directly fragmented in the mass analyser without needing further sub‐digestion reactions. Here we report the advantages of using multi‐stage ion trap mass spectrometry in the structural characterisation of haemoglobin alkylated with epichlorohydrin and diepoxybutane. Alkylated globins were digested with trypsin and the peptide mixtures were analysed by MS 3 . This technique allows the sequential fragmentation of peptides under analysis, giving rise to MS 3 product ion spectra with additional information with respect to MS 2 mass spectra. The results obtained complete the previously reported structural characterisation of alkylated haemoglobin, demonstrating the potential of ion trap mass spectrometry. Copyright © 2002 John Wiley & Sons, Ltd.