Fig. 5
From: Engineering mouse chymotrypsin B1 for improved trypsinogen degradation
Digestion of mouse cationic (T7) trypsinogen by wild-type mouse CTRB1, single mutants G236R and A244G, and double mutant G236R-A244G. (A) Reactions were analyzed by SDS-PAGE and Coomassie Blue staining. Representative gels are shown. (B) Trypsinogen cleavage was quantified by densitometry. The relative amount of the intact trypsinogen band was plotted as a function of time. The half-life values were calculated from semi-log plots. Data points represent the mean ± SD (n = 2). See “Materials & methods” for experimental details. The arrow indicates the intact, uncleaved protein.
