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Titlebook: Recombinant Technology in Hemostasis and Thrombosis; Leon W. Hoyer,William N. Drohan Book 1991 Springer Science+Business Media New York 19

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Interactions Between The Functional Domains of Antithrombin III occurs following cleavage of the Arg.-Ser. peptide bond and formation of a stable complex between this reactive site arginine of antithrombin III and the active site serine of the protease.. Antithrombin III is a member of a superfamily of protease inhibitors. designated as serine protease inhibito
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Protein C: Gene Structure and Protein Synthesisa feedback down-regulator of the coagulation cascade by specifically degrading the protein cofactors VIIIa and Va (Figure 1). The biological role of protein C and the vascular endothelium has been recently reviewed in a succinct fashion.. Protein C in a less understood manner also enhances the proce
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Molecular Defects in Hemophilia A, and when characterized by procoagulant or immunologic assays, it is a heterogeneous disorder. However, disease severity usually corresponds to the extent of factor VIII deficiency.. Severe hemophilia with recurrent hemarthroses usually means that there is no detectable plasma factor VIII (< 1% of
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Synthesis of Biologically Active Vitamin K-Dependent Coagulation Factors thrombosis. In particular, there has been interest in producing recombinant factor IX for treatment of hemophilia B, factor VII for treatment of hemophilia A patients with inhibitors and recombinant protein C for treatment of thrombotic disorders. Since these proteins undergo a unique posttranslati
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The Expression of Therapeutic Proteins in Transgenic Animals, albumin, immunoglobulins, fibrinogen and protein C are routinely isolated from human plasma. Improved protein isolation and viral inactivation techniques have led to the production of purer and safer plasma derivatives, although in some cases in quantities insufficient to meet patient needs.
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