ADSORPTION OF MONOCLONAL IGGS AND THEIR F(AB')(2) FRAGMENTS ONTO POLYMERIC SURFACES
ADSORPTION OF MONOCLONAL IGGS AND THEIR F(AB')(2) FRAGMENTS ONTO POLYMERIC SURFACES
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DOI：
10.1016/0927-7765(95)98205-2
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发表时间：
1995-09-25
影响因子：
5.8
通讯作者：
LYKLEMA, J
中科院分区：
文献类型：
--
作者：
BUIJS, J;LICHTENBELT, JWT;LYKLEMA, J
本文研究了两种单克隆免疫γ球蛋白（IgG）及其相应的F（ab '）（2）片段在三种聚合物胶乳上的吸附。这些胶乳中的两种是疏水性的，一种带正电荷，另一种带负电荷;第三种是带负电荷的亲水性胶乳。静电和疏水相互作用进行了系统的研究，通过进行吸附和电泳实验作为pH值和离子强度的函数，并通过使用两个不同的等电点的免疫球蛋白。蛋白质对疏水胶乳的亲和力几乎不受静电相互作用的影响。然而，在饱和水平的吸附量取决于整体的静电相互作用，导致在最大吸附量时，蛋白质的电荷部分由吸附剂表面电荷补偿。对于亲水性胶乳，当蛋白质被吸附剂表面静电排斥时，没有吸附。IgG和相应的F（ab '）（2）片段的吸附趋势相似，尽管有一些证据表明疏水相互作用和/或构象变化对F（ab'）（2）吸附不太重要。在疏水表面的蛋白质分子吸附主要在一个端上的取向，而对于带负电荷的亲水性乳胶和高的阳离子电荷密度的蛋白质，吸附量与一个紧密堆积的单层的侧上取向的蛋白质。
The present study deals with the adsorption of two monoclonal immune gamma globulins (IgGs) and their corresponding F(ab')(2) fragments onto three polymer latices. Two of these latices are hydrophobic, one being positively and the other negatively charged; the third is a negatively charged hydrophilic latex. Electrostatic and hydrophobic interactions were systematically studied by performing adsorption and electrophoresis experiments as a function of pH and ionic strength, and by using two IgCs which differ in isoelectric point. The affinity of the proteins for the hydrophobic latices was barely influenced by electrostatic interactions. However, at saturation level the adsorbed amounts were dependent on the overall electrostatic interaction, resulting in a maximum adsorbed amount when the protein charge is partly compensated by the sorbent surface charge. For the hydrophilic latex, there was no adsorption when the proteins were electrostatically repelled by the sorbent surface. The trends in the adsorption of IgG and the corresponding F(ab')(2) fragments were similar, although there was some evidence that hydrophobic interactions and/or conformational changes were less important for F(ab')(2) adsorption. At hydrophobic surfaces the protein molecules adsorbed mainly in an end-on orientation, whereas for a negatively charged hydrophilic latex and high cationic charge densities on the protein, the adsorbed amounts correlated with a close-packed monolayer of side-on oriented proteins.