Table 1.
The sTF2-219 mediated improvement in the amidolytic activity of fVIIa
STF2-219 | Maximal velocity mOD/min | Kd(app) nM |
---|---|---|
WT | 9.2 ± 0.4 | 2.9 ± 0.7 |
N199A | 8.0 ± 0.2 | 3.0 ± 0.5 |
R200A | 7.7 ± 0.2 | 3.2 ± 0.6 |
K201A | 7.3 ± 0.2 | 2.9 ± 0.7 |
The amidolytic function of 5 nM fVIIa toward SpVIIa in the presence of increasing concentrations of wild-type or mutant cofactors was determined in TBS/Ca2+ as described under “Materials and Methods”. All values are average of three measurements. The amidolytic activity of fVIIa in the absence of sTP2-219 was not significantly different from the background chromogenic substrate activity in the absence of the protease.