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1 at the productive recognition of factor X by Xase arises from a multistep reaction requiring an initi
2 activation of factor X by an enzyme complex (Xase) composed of the trypsin-like serine proteinase, fa
4 cognition of human factor X by the extrinsic Xase complex is not achieved through specific interactio
6 tely activated to factor Xa by the extrinsic Xase complex or by a purified activator from Russell's v
9 showed >9-fold increases in K(d) for factor Xase assembly, implicating these residues in stabilizing
14 3) in normal hemostasis the intrinsic factor Xase function contributes to the durability of the resup
15 resupply; 2) impairments in intrinsic factor Xase function, i.e. hemophilias A and B, result in an im
24 hibitor of the prothrombinase and the factor Xase complexes regardless of the degree of membrane curv
25 s to the K(m) for factor X binding to factor Xase, and this parameter is critical for activity assess
27 its ability to function within the intrinsic Xase complex to activate X may play a significant role i
28 pid, fVIIIa incorporation into the intrinsic Xase complex, thrombin generation in plasma, and fVIII u
29 eptor tissue factor (TF) or by the intrinsic Xase complex, which consists of active factors VIII (VII
32 sis for the protein substrate specificity of Xase using TF reconstituted into vesicles of phosphatidy
33 2 major complexes of the intrinsic pathway, Xase and prothrombinase, leading to a 20- and 10-fold in
34 C6 phosphatidylcholine, also accelerated the Xase complex, indicating that kcat enhancement has less
37 occupation of the active site of VIIa within Xase by a reversible inhibitor or an alternate peptidyl
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