人凝血因子VIII与血管性血友病因子之间的相互作用。因子VIII上高亲和力结合位点的特性。
The interaction between human blood-coagulation factor VIII and von Willebrand factor. Characterization of a high-affinity binding site on factor VIII.
作者信息
Leyte A, Verbeet M P, Brodniewicz-Proba T, Van Mourik J A, Mertens K
机构信息
Department of Blood Coagulation, Central Laboratory of The Netherlands Red Cross Blood Transfusion Service, Amsterdam.
出版信息
Biochem J. 1989 Feb 1;257(3):679-83. doi: 10.1042/bj2570679.
The interaction between human Factor VIII and immobilized multimeric von Willebrand Factor (vWF) was characterized. Equilibrium binding studies indicated the presence of multiple classes of Factor VIII-binding sites on vWF. The high-affinity binding (Kd = 2.1 x 10(-10) M) was restricted to only 1-2% of the vWF subunits. Competition studies with monoclonal antibodies with known epitopes demonstrated that the Factor VIII sequence Lys1673-Arg1689 is involved in the high-affinity interaction with vWF.
对人凝血因子VIII与固定化多聚体血管性血友病因子（vWF）之间的相互作用进行了表征。平衡结合研究表明vWF上存在多类凝血因子VIII结合位点。高亲和力结合（解离常数Kd = 2.1×10⁻¹⁰ M）仅局限于1 - 2%的vWF亚基。使用具有已知表位的单克隆抗体进行的竞争研究表明，凝血因子VIII序列Lys1673 - Arg1689参与了与vWF的高亲和力相互作用。
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