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Inhibition of human α- and γ-thrombin by A. gambiae cE5
The affinity for thrombin of the P5 fragment is comparable with that of full-length cE5. Disruption of thrombin's exosite I decreases the inhibition potency of cE5 (and P5) by 3 orders of magnitude. Ki values ± S.E. given are representative of two independent experiments.
| Inhibitor | α-Thrombin | γ-Thrombin |
|---|---|---|
| pm | nm | |
| cE5 | 5.50 ± 1.26 | 3.79 ± 0.16 |
| P5 fragment | 20.80 ± 0.99 | 10.99 ± 0.69 |
