Table 2.

Effects of varied protease inhibitors on the enzymatic activity of recombinant tryptase ϵ




% Inhibition
Inhibitor
Major specificity
Tryptase ϵ
Trypsin
Antipain   Papain and trypsin   77   99  
Bestatin   Amino peptidases   8   13  
Pepstatin   Aspartyl proteases   0   0  
Aprotinin   Serine proteases   5   100  
A1AT   Neutrophil elastase and TMT   0   95  
SLPI
 
Varied serine proteases
 
15
 
90
 



% Inhibition
Inhibitor
Major specificity
Tryptase ϵ
Trypsin
Antipain   Papain and trypsin   77   99  
Bestatin   Amino peptidases   8   13  
Pepstatin   Aspartyl proteases   0   0  
Aprotinin   Serine proteases   5   100  
A1AT   Neutrophil elastase and TMT   0   95  
SLPI
 
Varied serine proteases
 
15
 
90
 

The protease activity of the recombinant tryptase ϵ and trypsin was determined with synthetic substrate H-D-Leu-Thr-Arg-pNA in the presence of different inhibitors. The enzyme-protease inhibitor ratio used in these experiments was approximately 1:10. The experiment was done in duplicate; shown are the mean values. Similar findings were obtained in a second experiment.