TABLE 5.
Apparent equilibrium constants of the first step of slow-binding (K1) and the overall process (KI*) for the reversible probes.
| # | Trypsin-3 | β-tryptase | Thrombin | |||
|---|---|---|---|---|---|---|
| K1 (μM) a | KI* (μM) a | K1 (μM) a | KI* (μM) a | K1 (μM) a | KI* (μM) a | |
| 32b | N.D. b | N.D. b | N.D. b | N.D. b | 22.6 ± 5 | 0.45 ± 0.03 |
| 45b | N.D. b | N.D. b | N.D. b | N.D. b | 9.97 ± 1.0 | 1.14 ± 0.11 |
| 33b | N.D. b | N.D. b | N.D. b | N.D. b | 4.13 ± 0.7 | 0.28 ± 0.04 |
| 46b | N.D. b | N.D. b | N.D. b | N.D. b | 0.95 ± 0.2 | 0.07 ± 0.009 |
| 34b | 0.029 ± 0.005 | 0.003 ± 0.0003 | 15.8 ± 5 | 1.11 ± 0.09 | 134 ± 26 | 4.93 ± 0.51 |
| 50b | 0.098 ± 0.022 | 0.003 ± 0.0002 | 3.28 ± 0.5 | 0.41 ± 0.03 | * c | 1.55 ± 0.25 |
| 35b | 0.001 ± 0.0001 | 1 × 10−4 ± 1 × 10−5 | 3.20 ± 1.8 | 0.12 ± 0.01 | 32.7 ± 4 | 0.63 ± 0.04 |
| 52b | 0.017 ± 0.0005 | 0.001 ± 7 × 10−5 | 0.68 ± 0.07 | 0.06 ± 0.003 | * c | 0.62 ± 0.08 |
| 36b | 0.008 ± 0.0008 | 0.001 ± 0.0001 | 0.34 ± 0.07 | 0.09 ± 0.01 | 9.03 ± 0.5 | 0.03 ± 0.002 |
| 54b | 0.006 ± 0.0005 | 8 × 10−4 ± 3 × 10−5 | 0.13 ± 0.03 | 0.02 ± 0.001 | * c | 0.06 ± 0.006 |
aK1 and KI* are calculated from two independent experiments; when SD was higher than three times the average value, a third independent experiment was run (mean ± SD).
bN.D.: compounds have an irreversible mechanism of inhibition, K1 was not calculated.
c
K1 determination is not possible by curve fitting.