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.