Fulltext

Electron Transfer Dissociation Mass Spectrometry of Hemoglobin on Clinical Samples

Coelho Graça, Didia ; Lescuyer, Pierre ; Clerici, Lorella ; Tsybin, Yury ; Hartmer, Ralf ; Meyer, Markus ; Samii, Kaveh ; Hochstrasser, Denis ; Scherl, Alexander

In: Journal of The American Society for Mass Spectrometry, 2012, vol. 23, no. 10, p. 1750-1756

Ajouter à la liste personnelle
    Titre
    • Electron Transfer Dissociation Mass Spectrometry of Hemoglobin on Clinical Samples
    Auteur
    • Coelho Graça, Didia. Biomedical Proteomics Research Group, Department of Human Protein Science, Faculty of Medicine, Geneva University, Geneva, Switzerland
    • Lescuyer, Pierre. Biomedical Proteomics Research Group, Department of Human Protein Science, Faculty of Medicine, Geneva University, Geneva, Switzerland
    • Clerici, Lorella. Department of Genetic and Laboratory Medicine, Geneva University Hospitals, Geneva, Switzerland
    • Tsybin, Yury. Biomolecular Mass Spectrometry Laboratory, Ecole Polytechnique Fédérale de Lausanne, Lausanne, Switzerland
    • Hartmer, Ralf. Bruker Daltonics, Bremen, Germany
    • Meyer, Markus. Bruker Daltonics, Bremen, Germany
    • Samii, Kaveh. Division of Hematology, Geneva University Hospital, Geneva, Switzerland
    • Hochstrasser, Denis. Biomedical Proteomics Research Group, Department of Human Protein Science, Faculty of Medicine, Geneva University, Geneva, Switzerland
    • Scherl, Alexander. Biomedical Proteomics Research Group, Department of Human Protein Science, Faculty of Medicine, Geneva University, Geneva, Switzerland
    Type de document
    • Postprint
    Langue
    • Anglais
    Publié dans
    • Journal of The American Society for Mass Spectrometry, 2012, vol. 23, no. 10, p. 1750-1756. Springer-Verlag
    Autre version électronique
    Identifiant OAI-PMH
    • oai:doc.rero.ch:320863
    Summary
    A mass spectrometry-based assay combining the specificity of selected reaction monitoring and the protein ion activation capabilities of electron transfer dissociation was developed and employed for the rapid identification of hemoglobin variants from whole blood without previous proteolytic cleavage. The analysis was performed in a robust ion trap mass spectrometer operating at nominal mass accuracy and resolution. Subtle differences in globin sequences, resulting with mass shifts of about one Da, can be unambiguously identified. These results suggest that mass spectrometry analysis of entire proteins using electron transfer dissociation can be employed on clinical samples in a workflow compatible with diagnostic applications