Table 1.
AGE-modified peptides identified by MS analysis in high MW-species of BSA-glucose captured by VC1-resin.
| Modification | ΔM | Peptide sequencea | Amino acidb | Charge | MH+c | ppm |
|---|---|---|---|---|---|---|
| Schiff base | +132.04426 | AEFVEVTK*LVTDLTK | K256 | +3 | 1824.98307 | −0.60 |
| Deoxy-fructosyl-lysine | +162.05282 | ATEEQLK*TVMENFVAFVDK | K568 | +3 | 2361.15543 | +0.97 |
| QNCDQFEK*LGEYGFQNALIVR | K420 | +3 | 2691.27079 | −0.45 | ||
| ADLAK*YICDNQDTISSK | K285 | +3 | 2103.97409 | −0.49 | ||
| AEFVEVTK*LVTDLTK | K256 | +3 | 1854.99442 | −0.17 | ||
| SLHTLFGDELCK*VASLR | K100 | +4 | 2108.06777 | −0.73 | ||
| K*VPQVSTPTLVEVSR | K437 | +3 | 1801.98758 | −1.70 | ||
| NYQEAK*DAFLGSFLYEYSR | K346 | +3 | 2463.13309 | −0.82 | ||
| Tetra-hydro-pyridmidine | +144.04226 | YTR*KVPQVSTPTLVEVSR | R436 | +3 | 2204.19156 | −0.21 |
| Carboxymethyl | +58.00548 | AFDEK*LFTFHADICTLPDTEK | K528 | +3 | 2556.19626 | −0.05 |
| AEFVEVTK*LVTDLTK | K256 | +2 | 1750.94621 | −0.67 | ||
| HLVDEPQNLIK*QNCDQFEK | K412 | +3 | 2413.14438 | −0.40 | ||
| LVNELTEFAK*TCVADESHAGCEK | K75 | +3 | 2666.20639 | −0.37 | ||
| LSQK*FPKAEFVEVTK | K245 | +3 | 1808.97855 | −0.45 | ||
| K*QTALVELLK | K548 | +3 | 1200.72013 | +0.21 | ||
| K*VPQVSTPTLVEVSR | K437 | +3 | 1697.94120 | −1.24 | ||
| Carboxyethyl | +72.02113 | R*HPEYAVSVLLR | R360 | +3 | 1511.83170 | −0.82 |
The high MW species of BSA-Glucose (≥250 kDa) shown in Fig. 3A were subjected to in-gel digestion.
a
The K* or R* indicate the position of the modified residue.
b
The numbering refers to the amino acid residue in the sequence of the precursor of BSA (containing the signal peptide).
c
Experimentally determined monoisotopic mass.