[M + Fe − 5H]2− peptide ion composition verified by Fourier transform mass spectrometry accurate mass and tandem mass spectrometry analyses
A. Grey Craig, J. Paul Speir, S. Rosamilia, V. Fursey, Marcelina B. Lirazan
Abstract
A. Grey Craig, J. Paul Speir, S. Rosamilia, V. Fursey, Marcelina B. Lirazan
Abstract
Previously, the unusual ion composition [M + Fe - 5H]2- had been proposed as the major species observed when a gamma-carboxy glutamate-containing glyco-peptide was analyzed with electrospray ionization in the negative ionization mode. The sequence assignment of this highly post-translationally modified peptide was based on the mass analysis using a quadrupole ion trap together with information from both Edman and DNA sequencing. Because there was little precedent for the loss of five protons from a ferric cationized peptide, we utilized Fourier transform mass spectrometry accurate mass and tandem mass spectrometry analyses to verify the peptide ion composition.
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Previously, the unusual ion composition [M + Fe - 5H]2- had been proposed as the major species observed when a gamma-carboxy glutamate-containing glyco-peptide was analyzed with electrospray ionization in the negative ionization mode. The sequence assignment of this highly post-translationally modified peptide was based on the mass analysis using a quadrupole ion trap together with information from both Edman and DNA sequencing. Because there was little precedent for the loss of five protons from a ferric cationized peptide, we utilized Fourier transform mass spectrometry accurate mass and tandem mass spectrometry analyses to verify the peptide ion composition.
Key concepts: Chemistry, Protein mass spectrometry, Mass spectrometry, Top-down proteomics, Electrospray ionization, Fourier transform ion cyclotron resonance, Tandem mass spectrometry, Sample preparation in mass spectrometry