Table 2.
Candidate biomarkers selected for LC-SRM-MS analysis
| Protein name | UniProt Entry name |
FCa | VIPb | Protein functionc | Proteotypic peptided | Peptide molecular weight | Transitionsf | CE (V)h | |
|---|---|---|---|---|---|---|---|---|---|
| Precursor ion | Product ion | ||||||||
| m/zg | m/zg | ||||||||
| Apoliprotein C-II | APOC2 | 2.44 | 0.94 | Lipid transport | TYLPAVDEK | 1034.5 | 518.3 | 771.4 | 25 |
| 518.3 | 658.34 | 25 | |||||||
| Clusterin | CLU | 1.32 | 1.63 | Complement pathway, innate immunity | TLLSNLEEAK | 1118.8 | 559.4 | 790.4 | 20 |
| 559.4 | 903.5 | 20 | |||||||
| Complement C4-B | CO4-B | 1.08 | 1.57 | Complement pathway, innate immunity | VGDTLNLNLR | 1113.8 | 557.9 | 629.4 | 15 |
| 557.9 | 742.5 | 15 | |||||||
| Complement Component C9 | CO9 | 1.31 | 1.65 | Complement activation, classical pathway | VVEESELAR | 1030.5 | 516.27 | 704.35 | 25 |
| 516.27 | 833.4 | 25 | |||||||
| Alpha-2-HS-glycoprotein (Fetuin A) | FETUA | −1.14 | 1.46 | Acute-phase response | HTLNQIDEDK | 1196.6 | 598.9 | 845.4 | 20 |
| 598.9 | 958.2 | 20 | |||||||
| Mannan-binding lectin serine-protease | MASP2 | 1.72 | 0.50 | Lectin complement pathway, innate immunity | AGYVLHRe | 814.4 | 408.23 | 425.8 | 15 |
| 408.23 | 312.9 | 15 | |||||||
| Mannose-binding protein C | MBL2 | 3.30 | 0.62 | Lectin complement pathway, innate immunity | SPDGDSSLAASER | 1290.8 | 646.9 | 533.3 | 25 |
| 646.9 | 733.38 | 25 | |||||||
| N-acetylmuramoyl-L-alanine amidase | PGRP2 | 1.62 | 1.03 | Petidoglycan digestion, innate immunity | TFTLLDPK | 933.5 | 466.67 | 686.4 | 25 |
| 466.67 | 585.4 | 20 | |||||||
| Bovine Fetuin | FETUA-B | Internal Standard | TPIVGQPSIPGGPVR | 1474.8 | 737.9 | 582.3 | 25 | ||
| 737.9 | 879.5 | 25 | |||||||
aFC, fold change of protein plasma level in the global proteome study of the EPIC population.
bVIP, variable importance in the projection, PLS-DA analysis (global proteome study of the EPIC population).
cDeduced from UniProt database.
dAmino acid sequence of the peptide selected for quantitation by LC-SRM-MS.
eAlthough this peptide has only seven amino acid residues, it was selected for SRM analysis because it gave the best response.
fThe transition used for quantitation is shown in bold type; the other transition was used to maximise the specificity of the method.
gm/z, mass to charge ratio of the selected peptide.
hCE, collision energy.