TY - JOUR
T1 - Fragmentation of cationized phosphotyrosine containing peptides by atmospheric pressure MALDI/Ion trap mass spectrometry
AU - Moyer, Susanne C.
AU - VonSeggern, Christopher E.
AU - Cotter, Robert J.
N1 - Funding Information:
The authors thank the reviewers for their intellectual input regarding this manuscript. Funding for this work was provided by a contract (DABT63-99-1-0006) to RJC from the Defense Advanced Research Project Agency (DARPA). Support for SCM was provided by a NSF-GOALI grant (CHE 9634238). CEV is supported by a NIH Training Grant in Anti-Cancer Drug Development (CA 09243).
PY - 2003/6
Y1 - 2003/6
N2 - An investigation of phosphate loss from sodium-cationized phosphotyrosine containing peptide ions was conducted using liquid infrared (2.94 μm) atmospheric pressure matrix-assisted laser desorption/ionization (AP MALDI) coupled to an ion trap mass spectrometer (ITMS). Previous experiments in our laboratory explored the fragmentation patterns of protonated phosphotyrosine containing peptides, which experience a loss of 98 Da under CID conditions in the ITMS. This loss of 98 Da is unexpected for phosphotyrosine, given the structure of its side chain. Phosphate loss from phosphotyrosine residues seems to be dependent on the presence of arginine or lysine residues in the peptide sequence. In the absence of a basic residue, the protonated phosphotyrosine peptides do not undergo losses of HPO3 (Δ 80 Da) nor HPO3 + H2O (Δ 98 Da) in their CID spectra. However, sodium cationized phosphotyrosine containing peptides that do not contain arginine or lysine residues within their sequences do undergo losses of HPO3 (Δ 80 Da) and HPO3 + H2O (Δ 98 Da) in their CID spectra.
AB - An investigation of phosphate loss from sodium-cationized phosphotyrosine containing peptide ions was conducted using liquid infrared (2.94 μm) atmospheric pressure matrix-assisted laser desorption/ionization (AP MALDI) coupled to an ion trap mass spectrometer (ITMS). Previous experiments in our laboratory explored the fragmentation patterns of protonated phosphotyrosine containing peptides, which experience a loss of 98 Da under CID conditions in the ITMS. This loss of 98 Da is unexpected for phosphotyrosine, given the structure of its side chain. Phosphate loss from phosphotyrosine residues seems to be dependent on the presence of arginine or lysine residues in the peptide sequence. In the absence of a basic residue, the protonated phosphotyrosine peptides do not undergo losses of HPO3 (Δ 80 Da) nor HPO3 + H2O (Δ 98 Da) in their CID spectra. However, sodium cationized phosphotyrosine containing peptides that do not contain arginine or lysine residues within their sequences do undergo losses of HPO3 (Δ 80 Da) and HPO3 + H2O (Δ 98 Da) in their CID spectra.
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U2 - 10.1016/S1044-0305(03)00142-9
DO - 10.1016/S1044-0305(03)00142-9
M3 - Article
C2 - 12781459
AN - SCOPUS:0038149394
SN - 1044-0305
VL - 14
SP - 581
EP - 592
JO - Journal of the American Society for Mass Spectrometry
JF - Journal of the American Society for Mass Spectrometry
IS - 6
ER -