Literature DB >> 11948814

Ion trap mass spectrometry in the structural analysis of haemoglobin peptides modified by epichlorohydrin and diepoxybutane.

Nadia Miraglia1, Adriana Basile, Maria Pieri, Antonio Acampora, Livia Malorni, Beatrice De Giulio, Nicola Sannolo.   

Abstract

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.

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Year:  2002        PMID: 11948814     DOI: 10.1002/rcm.645

Source DB:  PubMed          Journal:  Rapid Commun Mass Spectrom        ISSN: 0951-4198            Impact factor:   2.419


  1 in total

1.  Quantitative analysis of N-terminal valine peptide adducts specific for 1,2-epoxy-3-butene.

Authors:  Nadia I Georgieva; Gunnar Boysen; Patricia B Upton; Karupiah Jayaraj; Avram Gold; James A Swenberg
Journal:  Chem Biol Interact       Date:  2006-06-03       Impact factor: 5.192

  1 in total

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