Dissociation Constant (kd) and the Number of the Phospholipids in the Binding Site (n) in the Interaction of Intact and Nicked β2GPI With CL
| Sample . | State . | kd (mol/L) . | n* . |
|---|---|---|---|
| Human β2GPI | Intact | ∼10−8 | 20 |
| Nicked | ∼10−7 | 60 | |
| Bovine β2GPI-151 | Intact | ∼10−8 | 20 |
| Nicked | ∼10−7 | 50 |
| Sample . | State . | kd (mol/L) . | n* . |
|---|---|---|---|
| Human β2GPI | Intact | ∼10−8 | 20 |
| Nicked | ∼10−7 | 60 | |
| Bovine β2GPI-151 | Intact | ∼10−8 | 20 |
| Nicked | ∼10−7 | 50 |
*Determined by fitting an experimental curve of percentage vs CL concentration obtained at 25°C in 10 mmol/L Tris-HCl (pH 7.5) containing 10 mmol/L NaCl to a theoretical curve, as described in Materials and Methods.
Kinetic parameters for bovine β2GPI were taken from Hagihara et al.11