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血管性血友病因子血小板结合结构域的修饰

Modification of the platelet-binding domain of von Willebrand factor.

作者信息

Silverman C, Mascelli M A, Karl D W, Kirby E P

出版信息

J Lab Clin Med. 1987 Jul;110(1):113-8.

PMID:3496407
Abstract

Radioiodinated Bolton-Hunter reagent was used at low specific activity to probe for the function and reactivity of amino groups on von Willebrand factor (vWF), a plasma protein involved in platelet responses to damaged endothelial surfaces. The platelet receptor for vWF contains a membrane protein termed glycoprotein Ib. Modification of only one or two amino groups per vWF subunit caused a 50% reduction in the platelet-agglutinating activity of vWF, and a decrease in its ability to bind to platelets. All multimeric forms of vWF are modified. Loss of platelet-agglutinating activity on modification of less than 2% of the amino groups on each vWF subunit suggests that the amino groups in the glycoprotein Ib-binding domain of vWF are both particularly reactive and essential for its function.

摘要

低比活度的放射性碘化博尔顿-亨特试剂被用于探究血管性血友病因子(vWF)上氨基的功能和反应活性,vWF是一种参与血小板对受损内皮表面反应的血浆蛋白。vWF的血小板受体包含一种称为糖蛋白Ib的膜蛋白。每个vWF亚基仅一两个氨基的修饰就导致vWF的血小板凝集活性降低50%,以及其与血小板结合能力的下降。vWF的所有多聚体形式均被修饰。每个vWF亚基上不到2%的氨基修饰就导致血小板凝集活性丧失,这表明vWF糖蛋白Ib结合域中的氨基既具有特别高的反应活性,又对其功能至关重要。

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