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.