Isolation and characterization of thrombin-activated human factor VIII.
作者： J.E. Curtis , S.L. Helgerson , E.T. Parker , P. Lollar
DOI: 10.1016/S0021-9258(17)37594-4
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摘要: Recombinant human factor VIII (fVIII) was activated by thrombin at pH 7.4, followed CM-Sepharose chromatography values ranging from 3.5 to 7.4. Optimal coagulant activity recovered 5.5 and associated with the isolation of an A1/A2/A3-C1-C2 heterotrimer. The stable -80 degrees C, but decayed slowly (t1/2 approximately 1 week) nonproteolytically room temperature or 4 C. fVIIIa preparation assayed in hemophilia A plasma only 20% that porcine VIIIa. However, its 75% a plasma-free assay, indicating is unstable relative during coagulation assay. first-order rate constant for spontaneous, nonproteolytic loss 7.4 decreased 8-fold fIXa phospholipid, stabilized when incorporated into intrinsic pathway X activation complex.
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