Skip to main content
. Author manuscript; available in PMC: 2008 Aug 21.
Published in final edited form as: Biochemistry. 2007 Feb 27;46(11):3193–3199. doi: 10.1021/bi6025193

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.