TABLE 1.
Dissociation constants for the binding of FPR-thrombin and FPR-batroxobin to fibrinogen, fibrin, and related fragments
The affinities of FPR-thrombin or FPR-batroxobin for immobilized fibrin(ogen), fibrinogen fragments, or peptides was determined using SPR. Kd values were determined by kinetic analysis of the binding sensorgrams. The interaction of thrombin with γA/γ′-fibrin(ogen) was analyzed using a two-site binding model. Each value represents the mean ± S.D. of two to three experiments. NB represents no binding.
| FPR-thrombin |
FPR-batroxobin Kd | ||
|---|---|---|---|
| Kd1 | Kd2 | ||
| μm | μm | μm | |
| γA/γA-Fibrinogen | 2.3 ± 0.3 | 0.6 ± 0.1 | |
| γA/γ′-Fibrinogen | 1.5 ± 0.1 | 0.05 ± 0.02 | 0.5 ± 0.04 |
| γA/γA-Fibrin | 2.0 ± 0.9 | 0.5 ± 0.9 | |
| γA/γ′-Fibrin | 2.1 ± 0.4 | 0.1 ± 0.06 | 0.5 ± 0.9 |
| Fragment D | NB | NB | |
| Fragment E | 3.2 ± 1.5 | 2.1 ± 0.5 | |
| NDSK | 3.0 ± 1.0 | 4.5 + 1.7 | |
| γ′-Peptide | 1.1 ± 0.1 | NB | |
| α(17–51)-Peptide | 2.2 ± 1.0 | >25 | |