The Affinity and Stoichiometry of Binding of Human Factor VI11 to von Willebrand Factor

نویسندگان

  • Bonno N. Bouma
  • Jan J. Sixma
چکیده

To study the interaction between factor Vlll and von Willebrand factor (vWF), binding experiments were performed using immobilized plasma vWF. Plasma was obtained from healthy donors and from patients with severe hemophilia A. For normal and hemophilic vWF, the dissociation constants (kd) for binding of factor Vlll to vWF were 0.21 & 0.04 and 0.22 2 0.05 nmol/L, respectively. At saturation, the stoichiometry was one factor Vlll molecule per 50 vWF monomers. In gel-filtration experiments, vWF was saturated by 23 times more factor VIII. However, when this FVIII-vWF complex was immobilized on microtiter plates, the ratio of factor Vlll/vWF decreased to the same ratio as in the solid-phase binding assay. To exclude any effect of antibody binding, colloidal

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تاریخ انتشار 2000