1. Electron Transfer Dissociation Mass Spectrometry of Hemoglobin on Clinical Samples
- Author
-
Alexander Scherl, Denis F. Hochstrasser, Didia Coelho Graca, Pierre Lescuyer, Lorella Clerici, Markus Meyer, Yury O. Tsybin, Kaveh Samii, and Ralf Hartmer
- Subjects
Proteomics ,Chromatography ,Chemistry ,Selected reaction monitoring ,Analytical chemistry ,Clinical proteomics ,Hemoglobin variants ,Mass spectrometry ,Tandem mass spectrometry ,Top-down proteomics ,Mass Spectrometry ,Single reaction monitoring ,Mass ,Electron-transfer dissociation ,Hemoglobins ,Protein Subunits ,Electron transfer dissociation ,Structural Biology ,Humans ,Ion trap ,Top-down mass spectrometry ,Hemoglobin ,ddc:576 ,Chromatography, High Pressure Liquid ,Spectroscopy - Abstract
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.