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. Author manuscript; available in PMC: 2013 Jul 21.
Published in final edited form as: Anal Chem. 2011 Jan 6;83(3):701–707. doi: 10.1021/ac100775s

Table 4.

Impact of considering additional amino acid modifications on global and individual protein iTRAQ ratios.

Protein changes relative to the 144KNt condition 144KNt 144KNt_144Y 144KNt_144C 144KNt_14K 144KNt_42K 144KNt_43K 144KNt_48C 144KNt_16M
1. Protein overlap #(%) 183(100%) 174 (95%) 173 (95%) 161 (88%) 163 (89%) 164 (90%) 172 (94%) 173 (95%)
2. Global iTRAQ 1.6 1.5 1.6 1.6 1.6 1.5 1.6 1.5
3. False positive IDs % 0 1.1 1.2 3.5 1.2 3.6 3.6 2.4
4. Proteins w. iTRAQ/2 #(%) 7 (4%) 8 (5%) 21 (13%) 19 (12%) 17 (10%) 10 (6%) 9 (5%)
5. Protein losses # 7 8 20 18 17 9 8
6. Protein gains #(%) 23 (13%) 6 (3%) 21 (13%) 34 (21%) 27 (16%) 10 (6%) 10 (6%)
7. Protein gains w. iTRAQ/2 # 4 1 1 4 6 1 1

Note: The row of “Proteins w. iTRAQ/2” refers to the #(%) of proteins with larger than 2-fold changes in iTRAQ ratios after enabling additional amino acid modifications, as denoted by entries in Appendix 1 with the ratio of iTRAQ ratios≥2 or ≤0.5. The row of “Protein losses #” is denoted by entries in Appendix 1 with the ratio of iTRAQ ratios = 0. The row of “Protein gains #(%)” refers to the #/(%) of proteins that were newly identified after enabling additional amino acid modifications, and are entries with iTRAQ≠0 listed at the bottom of Appendix 1. The row of “Proteins gains w. iTRAQ/2 #“ refers to proteins that were newly identified after enabling additional amino acid modifications, and are entries with iTRAQ≥2 or iTRAQ≤0.5 listed at the bottom of Appendix 1.