Skip to main content
. Author manuscript; available in PMC: 2013 Mar 2.
Published in final edited form as: J Proteome Res. 2012 Feb 15;11(3):1512–1520. doi: 10.1021/pr2003165

Table 2. Multiple sites of attachment of peptide amides reacted with iTRAQ reagent.

Peptide Theoretical [M+H]+ Observed [M+H]+ Observed iTRAQ tagsα % Relative Intensity
619-YASEGLSK (853)b 1141.6 1141.5 2 100.0
1285.7 1285.6 3 42.9
620-YPSEGLSK (879) 1167.6 1167.7 2 94.9
1311.7 1311.8 3 100.0
1455.8 1455.9 4 16.2
621-YWSEGLSK (968) 1256.6 1256.5 2 100.0
622-YYSEGLSK (946) 1233.6 1233.7 2 100.0
1377.7 1377.8 3 80.7
1521.8 1521.9 4 3.0
623-YESEYLSK (1017) 1161.5 1161.5 1 4.8
1305.6 1305.6 2 28.1
1449.7 1449.7 3 100.0
1593.8 1593.8 4 2.9
623 after hydroxylamine 1161.5 1161.5 1 2.6
1305.6 1305.6 2 100.0
679-ASEHASYG (820) 964.4 964.4 1 1.8
1108.5 1108.5 2 35.8
1252.6 1252.6 3 100.0
1396.7 1396.7 4 0.89
680-ASEHAYYG (896) 1040.4 1040.4 1 3.4
1184.5 1184.5 2 35.6
1328.6 1328.6 3 100.0
1472.7 1472.7 4 40.2
681-ASEHATYG (834) 1122.5 1122.5 2 17.1
1266.6 1266.6 3 100.0
1410.7 1410.8 4 0.47
681 after hydroxylamine 978.4 978.5 1 100.0
1122.5 1122.5 2 2.1
a

Determined using MALDI TOF/TOF.

b

Number before peptide sequence is an in-house reference number referred to in the text; number in parenthesis is [M+H]+ of unmodified peptide amide.