Analysis of glycosylphosphatidylinositol membrane anchors by electrospray ionization-mass spectrometry and collision induced dissociation

Christopher A. Redman, Brian N. Green, Jane E. Thomas-Oates, Vernon N. Reinhold, Michael A. J. Ferguson

    Research output: Contribution to journalArticlepeer-review

    17 Citations (Scopus)

    Abstract

    The multi-component nature of glycosylphosphatidylinositol membrane anchors makes the analysis of their structure complex. Nuclear magnetic resonance spectroscopy of delipidated glycosylphosphatidylinositol-peptide fractions can supply considerable information but requires relatively large quantities of material. High-sensitivity sequencing techniques are available for the oligosaccharide portions of glycosylphosphatidylinositol anchors, but there is no simple and generally applicable technique to complement this information. In this paper we describe the application of electrospray ionization-mass spectrometry and collision induced dissociation to study intact glycosylphosphatidylinositol-peptides from aTrypanosoma brucei variant surface glycoprotein. Collision of the [M + 4H]4+ pseudomolecular ions of two glycosylphosphatidylinositol-peptide glycoforms produced easily interpretable daughter ion spectra, from which detailed information on the lipid moiety, carbohydrate sequence and site of peptide attachment could be obtained. All of the collision induced dissociation cleavage events occurred in the glycosylphosphatidylinositol portion of the glycosylphosphatidylinositol-peptide. This technique supplies complementary data to the high-sensitivity oligosaccharide sequencing procedures and should greatly assist glycosylphosphatidylinositol anchor structure-function studies, particularly when sample quantities are limiting.
    Original languageEnglish
    Pages (from-to)187-193
    Number of pages7
    JournalGlycoconjugate Journal
    Volume11
    Issue number3
    DOIs
    Publication statusPublished - 1 Jan 1994

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