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. 2018 Nov 8;2018:6375379. doi: 10.1155/2018/6375379

Table 2.

Oxidative modification of proteins ubiquitously present in samples irrespective of storage. Modifications labeled with Ox or C represent either peptide oxidation or peptide carbonylation, respectively.

Accession Description Sequence Modification
Day 0 Day 14 Day 35
A0A0K2BMD8 Mutant hemoglobin alpha 2 globin chain VADALTNAVAHVDDMPNALSALSDLHAHK Ox Ox
P00558 Phosphoglycerate kinase 1 AHSSMVGVNLPQK Ox
IQLINNMLDK Ox Ox
SVVLMSHLGRPDGVPMPDK Ox
VNEMIIGGGMAFTFLK Ox
P02042 Hemoglobin subunit delta EFTPQMQAAYQK Ox
P02549 Spectrin alpha chain, erythrocytic 1 ADMEAEAPTFQALEDFSAELIDSGHHASPEIEK Ox, C Ox Ox
EKMEILDNNWTALLELWDER Ox Ox
FSSDFDELSGWMNEK Ox Ox, C Ox
LTLSHPSDAPQIQEMKEDLVSSWEHIR Ox, C
SDDKSSLDSLEALMK Ox Ox
P02730 Band 3 anion transport protein GLDLNGGPDDPLQQTGQLFGGLVR C
YTQEIFSFLISLIFIYETFSKLIKIFQDHPLQK C
PQGPLPNTALLSLVLMAGTFFFAMMLR Ox Ox
RYQSSPAKPDSSFYK Ox
P04075 Fructose-bisphosphate aldolase A IGEHTPSALAIMENANVLAR Ox
P04406 Glyceraldehyde-3-phosphate dehydrogenase WGDAGAEYVVESTGVFTTMEK Ox
P11166 Solute carrier family 2, facilitated glucose transporter member 1 QGGASQSDKTPEELFHPLGADSQV C
SFEMLILGR Ox
P11171 Protein 4.1 SMTPAQADLEFLENAK Ox Ox
P11277 Spectrin beta chain, erythrocytic DEEGAIVMLK Ox Ox
DGLNEMWADLLELIDTR Ox Ox
DLEDETLWVEER C C
ESQQLMDSHPEQK Ox
GLDAHLEQIFQEAHGMVAR Ox Ox
HQAFVAELASHEGWLENIDAEGK C
KEELGELFAQVPSMGEEGGDADLSIEK Ox, C
LWSYLQELLQSR Ox Ox
QLMDEKPQFTALVSQK C C Ox, C
VISDEIPKDEEGAIVMLK Ox
P16157 Ankyrin-1 DIEVLEGMSLFAELSGNLVPVKK Ox
EGQNANMENLYTALQSIDR Ox
GFTPLYMAAQENHLEVVK Ox
HGVMVDATTR Ox Ox
MGYTPLHVASHYGNIKLVK Ox, C
SLLQYGGSANAESVQGVTPLHLAAQEGHAEMVALLLSK Ox, C
TGASIDAVTESGLTPLHVASFMGHLPIVK Ox Ox
VETPLHMAAR Ox
P27105 Erythrocyte band 7 integral membrane protein EEIAHNMQSTLDDATDAWGIK Ox
NLSQILSDREEIAHNMQSTLDDATDAWGIK Ox Ox
P52209-2 Isoform 2 of 6-phosphogluconate dehydrogenase, decarboxylating YGPSLMPGGNK Ox
P60709 Actin, cytoplasmic 1 KDLYANTVLSGGTTMYPGIADR Ox