Ion mobility augments the utility of mass spectrometry in the identification of human hemoglobin variants

Jonathan P. Williams, Kevin Giles, Brian N. Green, James Scrivens, Robert H. Bateman

    Research output: Contribution to journalArticlepeer-review

    10 Citations (Scopus)

    Abstract

    The global dispersion of hemoglobin variants through population migration has precipitated a need for their identification. A particularly effective mass spectrometry (MS)-based procedure involves analysis of the intact globin chains in diluted blood to detect the variant through mass anomalies, followed by location of the variant amino acid residue by direct analysis of the enzymatically digested globins. Here we demonstrate the use of ion mobility separation in combination with this MSprocedure to reduce mass spectral complexity. In one example, the doubly charged tryptic peptide from a low abundance variant (4%) occurred at the same m/z value as a singly and a doubly charged interfering ion. In another example, the singly charged tryptic peptide from an α-chain variant (26%) occurred at the same m/z value as a doubly charged interfering ion. Ion mobility was used to separate the variant ions from the interfering ions, thus allowing the variant peptides to be observed and sequenced by tandem mass spectrometry.

    Original languageEnglish
    Pages (from-to)3179-3186
    Number of pages8
    JournalRapid Communications in Mass Spectrometry
    Volume22
    Issue number20
    DOIs
    Publication statusPublished - 30 Oct 2008

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