Inhibition Profile of α- and β-Tryptases
| Protease Inhibitor . | Percent Control . | ||
|---|---|---|---|
| . | β-Tryptase . | α-Tryptase . | α-Tryptase (Intracellular) . |
| . | (Secreted) . | (Secreted) . | . |
| — | 100 | 100 | 100 |
| EDTA (2 mmol/L) | 95 ± 0.5 | 92 ± 2.5 | 91 ± 1.6 |
| Soybean trypsin inhibitor (10 μg/mL) | 82 ± 0.2 | 85 ± 1.5 | 78 ± 2.8 |
| Aprotinin (10 μg/mL) | 30 ± 0.6 | 35 ± 2.5 | 33 ± 1.8 |
| Benzamidine (2 mmol/L) | 3.2 ± 0.5 | 4.5 ± 1.0 | 3.5 ± 1.2 |
| Leupeptin (0.2 mmol/L) | 1.5 ± 0.3 | 1.0 ± 0.4 | 1.5 ± 0.5 |
| Protease Inhibitor . | Percent Control . | ||
|---|---|---|---|
| . | β-Tryptase . | α-Tryptase . | α-Tryptase (Intracellular) . |
| . | (Secreted) . | (Secreted) . | . |
| — | 100 | 100 | 100 |
| EDTA (2 mmol/L) | 95 ± 0.5 | 92 ± 2.5 | 91 ± 1.6 |
| Soybean trypsin inhibitor (10 μg/mL) | 82 ± 0.2 | 85 ± 1.5 | 78 ± 2.8 |
| Aprotinin (10 μg/mL) | 30 ± 0.6 | 35 ± 2.5 | 33 ± 1.8 |
| Benzamidine (2 mmol/L) | 3.2 ± 0.5 | 4.5 ± 1.0 | 3.5 ± 1.2 |
| Leupeptin (0.2 mmol/L) | 1.5 ± 0.3 | 1.0 ± 0.4 | 1.5 ± 0.5 |
A total of 50 μL of the active recombinant tryptases were incubated with various known protease inhibitors for 15 minutes at 37°C. After incubation, proteolytic activity of the mixtures was compared to tryptase alone using TGPA and p-Nitroanilide generation determined at 405 nm. Activities are expressed as a percentage of maximum.