Structure of Membrane-Bound Porcine Factor VIII
نویسندگان
چکیده
منابع مشابه
Porcine factor VIII: pharmacoeconomics of inhibitor therapy.
The treatment of acquired haemophilia is characteristically exceedingly expensive and thus a cost-benefit analysis of the several available treatment strategies is urgently needed. To address this issue, decision-analysis techniques were used to construct a cost-minimization model to compare the cost of treatment with porcine factor VIII (pFVIII), human FVIII (hFVIII) or an activated prothrombi...
متن کاملFactor VIII structure and function.
Factor VIII, a non-covalent heterodimer comprised of a heavy chain (A1-A2-B domains) and light chain (A3-C1-C2 domains), circulates as an inactive procofactor in complex with von Willebrand factor. Metal ions are critical to the integrity of factor VIII, with Cu and Ca ions stabilizing the heterodimer and generating the active conformation, respectively. Activation of factor VIII catalyzed by t...
متن کاملPorcine recombinant factor VIII: an additional weapon to handle anti-factor VIII antibodies.
This review focuses on the use of recombinant porcine factor VIII (FVIII) for the treatment of bleeding episodes in patients with severe haemophilia A complicated by inhibitors and in those with acquired haemophilia A due to the onset of anti-FVIII autoantibodies. We present the main characteristics of recombinant porcine factor VIII (FVIII) and provide a summary of the published results of the...
متن کاملMolecular characterization of commercial porcine factor VIII concentrate.
Commercial porcine factor VIII concentrate (Hyate:C) is effective in treatment of patients with hemophilia A who have circulating antibodies to factor VIII. The molecular forms of factor VIII in the concentrate were identified and evaluated in light of the known properties of porcine and human factor VIII. The factor VIII in the concentrate was isolated by tandem chromatography on gelatin-Sepha...
متن کاملpH-dependent denaturation of thrombin-activated porcine factor VIII.
Thrombin-activated porcine factor VIII (fVIIIaIIa) is a stable, active, 160-kDa heterotrimer at concentrations exceeding 2 x 10(-7) M in 0.7 M NaCl, 0.01 M histidine Cl, 5 mM CaCl2, pH 6.0, at 4 degrees C or 20 degrees C. Two of the subunits, fVIIIA1 and fVIIIA2, are derived from the heavy chain of the plasma-derived, heterodimeric fVIII precursor. The third subunit, fVIIIA3-C1-C2, is derived f...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2013
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2012.11.1943