Skip to main content
. Author manuscript; available in PMC: 2012 Jul 1.
Published in final edited form as: Free Radic Biol Med. 2011 Mar 17;51(1):197–204. doi: 10.1016/j.freeradbiomed.2011.03.018

Fig. 3.

Fig. 3

Relative quantification of the identified selenocysteine peptide (residue 37 to 52 of GPX1) between SOD1−/− and WT by extracted ion chromatogram (XIC) analysis. Expanded view of XIC on a doubly-charged ion: [903.97]2+ for tryptic GPX1 peptide, VLLIENVASLUGTTIR acquired from WT sample at top panel (A) and from SOD1−/− mutant sample at bottom panel (B). The integrated peak areas at retention of 52 min plus those for the triply-charged ion of the same peptide (data not shown here) were used to determine the relative ratio changes between two samples. The same XIC approach was applied for the rest detected GPX1 tryptic peptides (see Table 2).