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. 2020 Jun 1;36:101592. doi: 10.1016/j.redox.2020.101592

Table 1.

Carbonylation of spectrin alpha and beta chains from RBC plasma membranes isolated from mice 24 h post-halogen exposure. Six putative carbonylation sites were confirmed by high resolution tandem mass spectrometry within spectrin alpha chain, and one site was identified within spectrin beta chain post-bromine exposure. These sites were all confirmed with a number of high confidence filters that included A-score and localization probabilities as indicated within the table, and further explained in detail within the methods section. The representative chromatography along with the MS1 & MS2 spectra are further highlighted in Fig. 4.

Spectrin Alpha Chain, Erythocytic Protein (P08032):
Peptide Carbonylation
Modification Site/Sequence
Tx Localization
Probability
A-score Peptide
Probability
Xcorr m/z Δppm
(K640) QQDFEEELAVNEIMLNNLEK Cl2 100% 1000 97% 4.1 3 −3.5
(K1401) GKCDQVESWMVAR Br2 100% 1000 99% 2.7 3 −0.6
(K1484) ALKEQLLTELGK Br2 100% 152 97% 2.7 2 −0.0
(K1706) MNGVNERFENVQSLAAAHHEK Cl2 100% 1000 99% 3.7 3 −2.9
(K1988) LSEIAELKDQLVAGEHSQAK* Br2 100% 165 100% 5.5 3 −1.7
(K2259) MQHNLEQQIQAKDTIGVSEETLKEFSTTYK Br2 100% 25 96% 3.3 5 −7.1
Spectrin Beta Chain, Erythocytic Protein (P15508):
Peptide
Modification Site/Sequence
Tx
Localization
Probability
A-score
Peptide
Probability
Xcorr
m/z
Δppm
(K960) VNNYCVDCEETSKWIMDK Br2 100% 88 100% 4.6 2 8.0