TABLE 2.
Mass spectrometric analysis of apoA-I proteolytic fragments produced by human or rat chymase in vitro
| Recombinant Human Chymase | Rat Chymase | |||||
| Apparent Molecular Mass | Molecular Mass | Cleavage site | Fragment | Molecular Mass | Cleavage Site | Fragment |
| 28 | 28,080 | — | 1-243 | 28,080 | — | 1-243 |
| 26 | 26,458 | Phe229 | 1-229 | — | — | — |
| 26 | 25,964 | Phe225 | 1-225 | — | — | — |
| 22 | 22,395 | Tyr192 | 1-192 | 22,395 | Tyr192 | 1-192 |
Aliquots of the reaction mixtures used for analysis on PAGE gel (see Fig. 5) were analyzed by mass spectrometry. Intact apoA-I (1-243) and apoA-I fragments generated by either human or rat chymase are shown. The analysis reveals that the 26 kDa band generated by human chymase contained two peptides of similar sizes, which comigrated on PAGE gel.