Zinc ions promote the binding of factor XII/factor XIIA to acidic phospholipids but have no effect on the binding of high-Mr kininogen.
Zinc ions promote the binding of factor XII/factor XIIA to acidic phospholipids but have no effect on the binding of high-Mr kininogen.
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锌离子促进因子XII/因子XIIA与酸性磷脂的结合，但对高Mr激肽原的结合没有影响。
DOI：
10.1111/j.1432-1033.1991.tb15912.x
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发表时间：
1991
期刊：
影响因子：
--
通讯作者：
T. Halkier
中科院分区：
文献类型：
--
作者：
I. Schousboe;T. Halkier
通过ELISA研究高Mr激肽原和因子XII/因子XIIa与聚苯乙烯微量滴定板上包被的磷脂的结合。高Mr激肽原和因子XII/因子XIIa都特异性地结合到磷脂表面。仅观察到与带负电荷的磷脂的结合。高Mr激肽原的结合不受锌离子存在的影响。在磷脂酰胆碱中磷脂酰肌醇磷酸的表面浓度为20%时，计算出高Mr激肽原结合的解离常数（kD）为10 nM。在锌离子存在下，结合的纯化α-因子XIIa的量可增加4-5倍。最低的锌离子浓度得到最大的结合是0.1 mM。α-因子XIIa的结合被抑制高先生激肽原。独立的存在下的锌离子或高先生激肽原，kD为7.9 nM的α-因子XIIa结合计算。前激肽释放酶的结合依赖于高Mr激肽原的存在和浓度。在含有抑肽酶的血浆中，高Mr激肽原的结合在锌离子的存在下被明显抑制，这是因子XII结合的先决条件。锌离子对高Mr激肽原结合的这种明显的抑制作用可能是由于增加了因子XII的结合，从而取代了高Mr激肽原。
Binding of high-Mr kininogen and factor XII/factor XIIa to phospholipids coated on to polystyrene microtiter plates was investigated by ELISA. Both high-Mr kininogen and factor XII/factor XIIa bound specifically to the phospholipid surface. Binding was observed to negatively charged phospholipids only. The binding of high-Mr kininogen was not affected by the presence of zinc ions. At a surface concentration of 20% phosphatidylinositol phosphate in phosphatidylcholine a dissociation constant (kD) of 10 nM for the binding of high-Mr kininogen was calculated. The amount of bound purified alpha-factor XIIa could be increased 4-5-fold in the presence of zinc ions. The lowest zinc ion concentration giving maximal binding was 0.1 mM. The binding of alpha-factor XIIa was inhibited by high-Mr kininogen. Independent of the presence of zinc ions or high-Mr kininogen, a kD of 7.9 nM was calculated for alpha-factor XIIa binding. The binding of prekallikrein was dependent upon the presence and the concentration of high-Mr kininogen. In plasma containing aprotinin, the binding of high-Mr kininogen was apparently inhibited in the presence of zinc ions, which was a prerequisite for the binding of factor XII. This apparently inhibitory effect of zinc ions on the binding of high-Mr kininogen was probably due to the increased binding of factor XII, which displaced high-Mr kininogen.