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Analytical Chemistry Chemical Cytometry Quantitates Superoxide

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Figure 2. (A) ESI-LTQ-CID-MS 2 product ion spectrum of the type 1 modified PPARR peptide (aa 195-209) [M + 2H + BuUrBu] 2+ at m/z<br />

945.47. (B) ESI-LTQ-MS 3 product ion spectrum of [M + 2H + BuUr] 2+ at m/z 902.94. $: signal not assigned.<br />

and, as such, originate from cleavage of the amide bond<br />

between the lysine ε-amine group and the cross-linker.<br />

Offline Nano-HPLC/MALDI-TOF/TOF Mass Spectrometry.<br />

To ensure and to probe the general applicability of 1 for<br />

both ESI- and MALDI-MS, we additionally examined the frag-<br />

(39) Müller, M. Q.; de Koning, L. J.; Schmidt, A.; Ihling, C.; Syha, Y.; Rau, O.;<br />

Mechtler, K.; Schubert-Zsilavecz, M.; Sinz, A. J. Med. Chem. 2009, 52,<br />

2875–2879.<br />

6964 <strong>Analytical</strong> <strong>Chemistry</strong>, Vol. 82, No. 16, August 15, 2010<br />

mentation behavior of the cross-linker in the higher kinetic energy<br />

regime of collision activation (kinetic energy of the precursor ion<br />

in TOF/TOF-CID Ekin ≈ 1 keV) 40-42 in MALDI-TOF/TOF (ISD<br />

and CID) experiments. In the same fashion as for low-energy ESI-<br />

LTQ-orbitrap-MS n product experiments (kinetic energy of the<br />

precursor ion in LTQ-CID Ekin ≈ 1 eV) 43,44 Munc13-1 and PPARR<br />

peptides were created by tryptic digestion and separated by nano-<br />

HPLC before MS analysis.

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