Table 2. Binding constants for TGF-β3 and variants to the betaglycan endoglin-like domain.
| Surface | Analyte | Dissassociation constant (μM) |
|||
|---|---|---|---|---|---|
| Buffer suppl. | Kd (μM) | Rmax (RU) | Norm Rmax | ||
| TGF-β3 WW | BGe | None | 3.5±0.4 | 700±30 | 1.00±0.05 |
| TGF-β3 WD | BGe | None | 2.0±0.2 | 1000±100 | 1.00±0.04 |
| TGF-β3 DD | BGe | None | 5.6±0.2 | 1600±100 | 1.00±0.02 |
| TGF-β3 WW | TβRII | None | 1.2±0.1 | 330±10 | 0.47±0.02 |
| TGF-β3 WD | TβRII | None | 0.60±0.10 | 190±10 | 0.19±0.02 |
| TGF-β3 DD | TβRII | None | NDa | NDa | NDa |
| TGF-β3 WW | TβRI | 4 μM TβRII | 0.27±0.05 | 270±50 | 0.39±0.02 |
| TGF-β3 WD | TβRI | 4 μM TβRII | 0.30±0.05 | 150±10 | 0.15±0.01 |
| TGF-β3 DD | TβRI | 4 μM TβRII | NDa | NDa | NDa |
| aNot determined due to weak binding. | |||||