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1 competitive inhibitor of PF-3688 cleavage by Xase.
2 at the productive recognition of factor X by Xase arises from a multistep reaction requiring an initi
3 activation of factor X by an enzyme complex (Xase) composed of the trypsin-like serine proteinase, fa
4 s in the presence of calcium ions (extrinsic Xase complex).
5 cognition of human factor X by the extrinsic Xase complex is not achieved through specific interactio
6 te recognition and cleavage by the extrinsic Xase complex is unclear.
7 tely activated to factor Xa by the extrinsic Xase complex or by a purified activator from Russell's v
8 (fX) by factor VIIa (fVIIa) in the extrinsic Xase pathway.
9 gulation without input from extrinsic factor Xase activity.
10  showed >9-fold increases in K(d) for factor Xase assembly, implicating these residues in stabilizing
11 ts Ki for inhibition of the intrinsic factor Xase (105 microM).
12                         The intrinsic factor Xase complex (FXase) is comprised of a serine protease,
13 in potent inhibition of the intrinsic factor Xase complex.
14 or at two levels within the intrinsic factor Xase complex.
15 3) in normal hemostasis the intrinsic factor Xase function contributes to the durability of the resup
16 resupply; 2) impairments in intrinsic factor Xase function, i.e. hemophilias A and B, result in an im
17 nhibition of factor VIIIa-factor IXa (factor Xase) enzyme complex.
18 ed by the activity of a reconstituted factor Xase system.
19         The first assay reconstituted factor Xase using varying concentrations of A2 mutant and fixed
20 lso enhanced activity of fVIII in the factor Xase complex by two- to fourfold.
21       The catalytic activities of the factor Xase complex composed of the hemophilia A-associated FVI
22 is necessary for full activity of the factor Xase complex.
23 s as a cofactor for factor IXa in the factor Xase complex.
24 participation in the formation of the factor Xase complex.
25 hibitor of the prothrombinase and the factor Xase complexes regardless of the degree of membrane curv
26 s to the K(m) for factor X binding to factor Xase, and this parameter is critical for activity assess
27 p critical to interaction with factor IXa in Xase.
28 l interaction between factor X and intrinsic Xase occurs at exosites distant from the active site, fo
29 rce the distinctive specificity of intrinsic Xase for its biological substrate.
30 ulation factor X activation by the intrinsic Xase complex by showing that exosite binding plays a cri
31 the recognition of factor X by the intrinsic Xase complex occurs through a multistep "dock-and-lock"
32 its ability to function within the intrinsic Xase complex to activate X may play a significant role i
33         Factor X activation by the intrinsic Xase complex, composed of factor IXa bound to factor VII
34 kely dysfunctional assembly of the intrinsic Xase complex, resulting in hemophilia B (HB).
35 pid, fVIIIa incorporation into the intrinsic Xase complex, thrombin generation in plasma, and fVIII u
36 eptor tissue factor (TF) or by the intrinsic Xase complex, which consists of active factors VIII (VII
37 I or IX, the two components of the intrinsic Xase complex.
38 ) on anionic membranes to form the intrinsic Xase enzyme complex, responsible for activating FX in th
39 tive site but does not alter the affinity of Xase for factor X.
40 sis for the protein substrate specificity of Xase using TF reconstituted into vesicles of phosphatidy
41 tions between factor X and extended sites on Xase in determining substrate affinity.
42  2 major complexes of the intrinsic pathway, Xase and prothrombinase, leading to a 20- and 10-fold in
43 C6 phosphatidylcholine, also accelerated the Xase complex, indicating that kcat enhancement has less
44        An alternative approach to bypass the Xase complex is to inhibit endogenous anticoagulant acti
45 ity of interaction between components of the Xase complex, activated factors VIII and IX.
46 studies confirmed the binding of factor X to Xase assembled with IXa with a covalently blocked active
47 cted to engage the active site of IXa within Xase, acted as a classical competitive inhibitor of fact
48 occupation of the active site of VIIa within Xase by a reversible inhibitor or an alternate peptidyl
49 ractions with the active site of VIIa within Xase.