Effect of mutants in C1 domain on affinity for phospholipid vesicles and VWF
| Factor VIII . | Dissociation constants . | |
|---|---|---|
| Phospholipid,* μM . | VWF,† nM . | |
| Wild-type | 15 ± 6 | 0.94 ± 0.17 |
| 2090/2091 | > 200 | 0.56 ± 0.15 |
| 2092/2093 | > 200 | 0.43 ± 0.10 |
| 2159 | 134 ± 53 | > 100 |
| 2042/2043 | > 200 | 2.3 ± 1.5 |
| Factor VIII . | Dissociation constants . | |
|---|---|---|
| Phospholipid,* μM . | VWF,† nM . | |
| Wild-type | 15 ± 6 | 0.94 ± 0.17 |
| 2090/2091 | > 200 | 0.56 ± 0.15 |
| 2092/2093 | > 200 | 0.43 ± 0.10 |
| 2159 | 134 ± 53 | > 100 |
| 2042/2043 | > 200 | 2.3 ± 1.5 |
KD ± SD of fit. Normalized binding curves from 2 experiments with vesicles of 15% PS were averaged and fitted by nonlinear, least squares analysis.
KD ± SD of fit. Displacement curves from 3 competition, solution phase VWF-binding assays were averaged and fitted by nonlinear, least squares analysis. The concentration of VWF was analyzed as the VWF subunit concentration, assuming an Mr of 220 000.