. Author manuscript; available in PMC: 2009 Oct 3.

Published in final edited form as: Anal Chim Acta. 2008 Jun 5;627(1):117–128. doi: 10.1016/j.aca.2008.05.074

Table 1.

Sequences of model substrates employed in the study: bovine erythrocytes ubiquitin (UBQ), bovine erythrocytes carbonic anhydrase II (CA), and human placenta pi-class gluthatione S-transferase (GST). Arginine residues are highlighted as possible alkylation sites.

Protein	Statistics	Sequence
UBQ	76 residues 4 arginines 8559.62 Da	MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGG
CA	259 residues 9 arginines 28964.67 Da	SHHWGYGKHN GPEHWHKDFP IANGERQSPV DIDTKAVVQD PALKPLALVY GEATSRRMVN NGHSFNVEYD DSQDKAVLKD GPLTGTYRLV QFHFHWGSSD DQGSEHTVDR KKYAAELHLV HWNTKYGDFG TAAQQPDGLA VVGVFLKVGD ANPALQKVLD ALDSIKTKGK STDFPNFDPG SLLPNVLDYW TYPGSLTTPP LLESVTWIVL KEPISVSSQQ MLKFRTLNFN AEGEPELLML ANWRPAQPLK NRQVRGFPK
GST	209 residues 8 arginines 23209.98 Da	PPYTVVYFPV RGRCAALRML LADQGQSWKE EVVTVETWQE GSLKASCLYG QLPKFQDGDL TLYQSNTILR HLGRTLGLYG KDQQEAALVD MVNDGVEDLR CKYISLIYTN YEAGKDDYVK ALPGQLKPFE TLLSQNQGGK TFIVGDQISF ADYNLLDLLL IHEVLAPGCL DAFPLLSAYV GRLSARPKLK AFLASPEYVN LPINGNGKQ