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1 PCPS markedly accelerated the initial rate of prethrombi
2 avage of the factor Va heavy chain (with APC-PCPS) at Arg505, Arg662 and Arg306 results in a drastic
3 that, albeit with different timing, both FXa/PCPS and E coli infusion led to robust thrombin and plas
4 a strong burst of thrombin and plasmin, FXa/PCPS infusion did not produce measurable levels of compl
5 es a maximum value of 18 pM/s at 5-20 microM PCPS; further increases in the levels of PCPS decrease t
7 of prethrombin-2 by E2-fXa in the absence of PCPS, they are ineffective competitors in the presence o
10 for factor VII activation in the presence of PCPS at optimal concentrations vary from 1.2 microM for
12 ssay (with or without APC) with platelets or PCPS vesicles added to induce clot formation indicated t
13 phosphatidylserine, 75% phosphatidylcholine, PCPS) were evaluated using sedimentation velocity/equili
14 e of phosphatidylcholine-phosphatidylserine (PCPS) vesicles or purified human plasma lipoproteins.
15 (FXa/phosphatidylcholine-phosphatidylserine [PCPS]) vs LD100 Escherichia coli We found that, albeit w
16 y 0.05 nM factor Xa is anionic phospholipid (PCPS) dependent and achieves a maximum value of 18 pM/s
17 about proteasome-catalyzed peptide splicing (PCPS), the emerging rules governing this process, and th
21 mation using increasing concentrations of TF/PCPS or TF/PC in the presence of TFPI yielded families o
23 results suggest that interaction of fVa with PCPS improves the affinity of the activation complex for
24 he interaction of the Gla domain of fXa with PCPS also induces conformational changes in the protease
25 e of prethrombin 2 cleavage by the factor Xa-PCPS binary complex was increased by a factor of approxi
27 rating concentrations of factor Va to the Xa-PCPS binary complex led to increases in catalytic effici
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