TABLE 1.
Kinetic parameters for Pg activation by tPA in the presence of γ′-Fn or γA-Fn
Fn was formed by clotting 7 μm of γ′-Fg or γA-Fg with 5 nm thrombin or 3 units/ml batroxobin. Pg activation was quantified by monitoring S-2251 hydrolysis, and activation rates were determined to obtain the kcat and Km values. Values represent mean ± S.D. of at least three separate experiments.
| Thrombin |
Batroxobin |
|||
|---|---|---|---|---|
| kcat | Km | kcat | Km | |
| s−1 | μm | s−1 | μm | |
| γA-Fn | 0.129 ± 0.033 | 0.14 ± 0.02 | 0.161 ± 0.088 | 0.12 ± 0.01 |
| γ′-Fn | 0.151 ± 0.028 | 0.14 ± 0.03 | 0.146 ± 0.088 | 0.11 ± 0.03 |