Table 1.
SRM transitions and parameters used in this study.
| Compound Name | Sequence | Precursor Ion (m/z) | Product Ion (m/z) | Dwell Time (msec) | Collision Energy (V) |
|---|---|---|---|---|---|
| Leu-enkephalin | [YGGFL+H]+ | 556.3 | 397.2 (a4+) | 25 | 19 |
| 556.3 | 425.2 (b4+) | 25 | 16 | ||
| 556.3 | 278.1 (b3+) | 25 | 25 | ||
| Angiotensin II | [DRVYIHPF+2H]2+ | 523.8 | 263.1 (y2+) | 25 | 20 |
| 523.8 | 784.4 (b6+) | 25 | 18 | ||
| 523.8 | 647.4 (b5+) | 25 | 22 | ||
| Kemptide | [LRRASLG+2H]2+ | 386.7 | 567.3 (b5+-NH3) | 25 | 18 |
| 386.7 | 409.3 (b3+-NH3) | 25 | 25 | ||
| 386.7 | 539.4 (a5+-NH3) | 25 | 22 | ||
| BSA peptide I | [LVNELTEFAK+2H]2+ | 582.3 | 951.5 (y8+) | 25 | 18 |
| 582.3 | 595.3 (y5+) | 25 | 20 | ||
| 582.3 | 837.4 (y7+) | 25 | 16 | ||
| BSA peptide II | [HLVDEPQNLIK+2H]2+ | 653.4 | 712.4 (y6+) | 25 | 26 |
| 653.4 | 251.2 (b2+) | 25 | 26 | ||
| 653.4 | 1056.7 (y9+) | 25 | 23 | ||
| BSA peptide III | [CCTESLVNR+2H]2+ | 512.7 | 637.2 (b6+) | 25 | 17 |
| 512.7 | 581.7 (a6+- 28) | 25 | 16 |
The bolded transitions indicate the transition used for quantification of each peptide. The non bolded/italicized transitions were used to confirm the peptide's identity. The italicized transition of BSA peptide was used to monitor the platform's reproducibility and calibration.