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Identification of Low-Level Oxidation Products in Calmodulin Using NanoSpray ,,, Ion Trap Mass Spectrometry

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Figure 2B. Full-scan MS3 spectrum of doubly-charged ion at m/z 1177.5 for peak at RT 45.87 min.

In contrast, the MS2 spectrum of the doubly charged ion at m/z 1209.5 for the peak at RT = 49.45 min includes y and b-series ions, as well as the MetSO associated neutral loss for the b ions, indicating that the MetSO is located at the Nterminus of the peptide, e.g., Met109 (Figure 3A and Figure 3A insert). MS3 analysis of the peak at m/z 1177.4 in the MS2 spectrum substantiates oxidation of Met109 through the detection of MetSO-specific neutral loss sequence ions of Nterminal origin (Figure 3B).

Similarly, MS2 and MS3 experiments were conducted for the peak at RT = 56.31, and it was established that the corresponding peptide contained MetSO exclusively at Met144. The extent and character of MetSO formation in CaM shown in this experiment is in agreement with results published previously2.


Figure 3A. Full-scan MS2 spectrum of doubly-charged ion at m/z 1209.5 for peak at RT 49.45 min.
Insert: Amino acid sequence of T12 fragment indicating major C- and Nterminal fragment ions detected by full-scan MS2.




Figure 3B. Full-scan MS3 spectrum of doubly-charged ion at m/z 1177.5 for peak at RT 49.45 min.

Conclusions

The identification of low-level oxidation products such as MetSO in proteins and peptides can be easily achieved using any Thermo Finnigan LCQ series ion trap mass spectrometer with MSn capability. The combination of D
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