摘要
目的:研究人免疫球蛋白质与羧甲基葡聚糖的氨基偶联及其与其他蛋白质的特异结合作用。方法:测定不同条件下人免疫球蛋白G(IgG)在羧甲基葡聚糖表面静电吸附的影响,并采用氨基偶联的方法,将其交联固定于葡聚糖表面,测定其与羊抗人IgG的特异结合。结果:pH及离子强度对蛋白质在羧甲基葡聚糖表面静电吸附有较大的影响,流体速度控制蛋白质的静电吸附动力学过程,并对其静电吸附量产生影响,其与羊抗人IgG有很强的特异结合作用,表现为快结合慢解离的动力学过程。结论:3.0<pH<pI,弱的离子强度及传质过程控制流速下有利于蛋白质在羧甲基葡聚糖表面的吸附,并得到较高偶联的蛋白质量,人IgG与羊抗人IgG有很强的特异结合作用。
Aim： To study that human IgG protein couples with carboxylmethyl dextran by amine coupling reaction, and associates with goat anti-human IgG protein. Methods： The electrostatic adsorption of human IgG on the carboxylmethyl dextran surface was detected in different conditions, and human IgG was coupled with carboxylmethyl dextran by amine coupling reaction, and RU change was detected before association and after dissociation. The reaction was detected between human IgG and Goat anti-human IgG. Results： It is important for pH and ion strength to impact on the electrostatic adsorption of human IgG, and the flow rate determines the electrostatic adsorption dynamic process. Goat anti- human IgG and human IgG is rapidly associated and slowly dissociated. Conclusion ： When 3.0 〈 pH 〈 pI, weak ion strength and mass transport and under control, protein tend to be adsorb on the carboxylmethyl dextran surface and has a satisfying couple mass by amine coupling reaction. The association between Goat anti- human IgG and human IgG is rapid and strong.
出处
《北京联合大学学报》
CAS
2007年第3期57-61,共5页
Journal of Beijing Union University
基金
北京市教委科技发展重点项目
北京市自然科学基金重点项目资助(KZ200311417015)
