Effect of A2 domain stabilization on specific activities and kinetic parameters
| Protein . | aPTT, U/µg . | Chromogenic assay, U/µg . | K1/2 FVIIIa, nM* . | K1/2 FIXa, nM* . | Km, nM* . | Kcat, s-1* . |
|---|---|---|---|---|---|---|
| BDD-FVIII | 7.00 ± 2.35 (n = 3) | 6.87 ± 1.58 (n = 4) | 2.08 ± 0.40 | 1.62 ± 0.62 | 9.95 ± 0.65 | 1.48 ± 0.02 |
| D519V/E665V | 6.55 ± 1.34 (n = 2) | 12.58 ± 2.55 (n = 6) | 0.74 ± 0.10 | 0.43 ± 0.09 | 11.77 ± 0.82 | 1.87 ± 0.03 |
| Protein . | aPTT, U/µg . | Chromogenic assay, U/µg . | K1/2 FVIIIa, nM* . | K1/2 FIXa, nM* . | Km, nM* . | Kcat, s-1* . |
|---|---|---|---|---|---|---|
| BDD-FVIII | 7.00 ± 2.35 (n = 3) | 6.87 ± 1.58 (n = 4) | 2.08 ± 0.40 | 1.62 ± 0.62 | 9.95 ± 0.65 | 1.48 ± 0.02 |
| D519V/E665V | 6.55 ± 1.34 (n = 2) | 12.58 ± 2.55 (n = 6) | 0.74 ± 0.10 | 0.43 ± 0.09 | 11.77 ± 0.82 | 1.87 ± 0.03 |
Kcat, constant for catalytic turnover; Km, Michaelis constant.
From kinetic assays. K1/2, the apparent dissociation constant, is calculated as described in Gale et al.5