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. Author manuscript; available in PMC: 2012 Oct 19.
Published in final edited form as: J Proteomics. 2011 Apr 15;74(11):2510–2521. doi: 10.1016/j.jprot.2011.04.007

Figure 3. LC-MS/MS analysis the nitrated and unmodified peptide YLYEIAR and its unmodified counterpart by the QSTAR Elite and LTQ Velos.

Figure 3

A) MS/MS of the unmodified peptide YLYEIAR (MH22+, 464.3 m/z) from albumin detected by the QSTAR Elite. B) The MS/MS spectra of the 3NT modified peptide Y(NO2)LY(NO2)EIAR (MH22+, 509.2 m/z) from the QSTAR Elite and C) LTQ Velos. The Y and 3NT immonium ions are highlighted in bold as well as the y5 and b2 ions which are increased in mass due to the presence of the 3NT modification. Inset: Extracted ion chromatogram of the nitrated and unmodified peptide demonstrating the increased retention time that occurs after 3NT modification.