The Affinity and Stoichiometry of the Factor VIII/vWF Interaction
| . | KD (nmol/L) . | n . | Factor VIII/vWF (molecules/subunit) . | n . |
|---|---|---|---|---|
| vWF* | 0.94 ± 0.27 | 7 | 0.99 ± 0.14 | 2 |
| vWF† | 0.68 ± 0.28 | 8 | 0.9 ± 0.1 | 8 |
| wt-vWF† | 1.05 ± 0.05 | 2 | 0.8 ± 0 | 2 |
| ΔPro-vWF* | 4.95 ± 1.3 | 3 | 1.37 ± 0.42 | 3 |
| ΔPro-vWF† | 6.37 ± 0.6 | 4 | 0.85 ± 0.15 | 4 |
| . | KD (nmol/L) . | n . | Factor VIII/vWF (molecules/subunit) . | n . |
|---|---|---|---|---|
| vWF* | 0.94 ± 0.27 | 7 | 0.99 ± 0.14 | 2 |
| vWF† | 0.68 ± 0.28 | 8 | 0.9 ± 0.1 | 8 |
| wt-vWF† | 1.05 ± 0.05 | 2 | 0.8 ± 0 | 2 |
| ΔPro-vWF* | 4.95 ± 1.3 | 3 | 1.37 ± 0.42 | 3 |
| ΔPro-vWF† | 6.37 ± 0.6 | 4 | 0.85 ± 0.15 | 4 |
Factor VIII binding to vWF was studied either by immobilizing plasma-derived vWF (*) on Superose-12 beads or using a competition assay (*†) in which factor VIII binding to lipospheres was displaced by adding increasing amounts of vWF.
Abbreviations: wt-vWF, recombinant vWF; ΔPro-vWF, propeptide deleted vWF; n, number of determinations.