Kinetics and Affinity of FVlla Binding to TF
| Immobilized . | Ligand . | kassoc × 10−5 . | kdiss × 103 . | KD . |
|---|---|---|---|---|
| Protein . | . | (M−1s−1) . | (s−1) . | (nmol/L) . |
| BEGR-FVlla* | sTF | 3.4 ± 0.8 | 2.1 ± 0.1 | 6.3 ± 1.2 |
| BEGR-FVlla | hTFAA | 3.5 ± 0.8 | 1.7 ± 0.1 | 4.2 ± 1.2 |
| BEGR-FVlla | rTFAA | 2.1 | 2.7 | 12.9 |
| Immobilized . | Ligand . | kassoc × 10−5 . | kdiss × 103 . | KD . |
|---|---|---|---|---|
| Protein . | . | (M−1s−1) . | (s−1) . | (nmol/L) . |
| BEGR-FVlla* | sTF | 3.4 ± 0.8 | 2.1 ± 0.1 | 6.3 ± 1.2 |
| BEGR-FVlla | hTFAA | 3.5 ± 0.8 | 1.7 ± 0.1 | 4.2 ± 1.2 |
| BEGR-FVlla | rTFAA | 2.1 | 2.7 | 12.9 |
FVlla was modified with a biotinylated active site peptide chloromethyl ketone and captured on a streptavidin derivatized sensor chip as previously described.22 Changes in kinetic parameters must be greater than twofold to be considered significant.9