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. 2019 May 23;24:101226. doi: 10.1016/j.redox.2019.101226

Fig. 3.

Fig. 3

Number of sites of Trp (W) and Tyr (Y) modification (vertical axes) detected on laminin-111 after exposure to ONOOH. Isolated laminin-111 was exposed to ONOOH in concentrations ranging from equimolar to 500-fold molar excess (as indicated on the horizontal axes) for 20 min at 37 °C, with the resulting modified peptides detected by LC-MS using chromatographic and precursor mass features from the 500-fold molar excess samples used as a template. Panel A): Number of nitration sites detected by LC-MS at different concentrations of ONOOH at Trp (upper left panel), Tyr (upper right) and all residues (lower panel). Panel B): Number of di-nitration sites detected by LC-MS at different concentrations of ONOOH at Trp (upper left panel), Tyr (upper right panel) and all residues (lower panel). Only modifications detected in all three independent replicates from ONOOH treatment, and none of the control samples are included; statistical analysis is therefore not appropriate.