Kondo A, Kawano T, Itoh F, Higashitani K
Applied Chemistry Department, Kyushu Institute of Technology, Kitakyushu, Japan.
J Immunol Methods. 1990 Dec 31;135(1-2):111-9. doi: 10.1016/0022-1759(90)90263-u.
The influence of the properties of antigens and particles on the immunological agglutination kinetics of the antigen-coated latex particles was studied. Horse cytochrome c, hen egg-white lysozyme (HEL), bovine serum albumin (BSA), and Aspergillus sp. glucose oxidase were physically adsorbed onto the surfactant free latices of styrene-methacrylic acid (MAA) copolymer (P (S/MAA)) and polystyrene (PS). The initial rates of the immunological agglutination of these protein-coated particles initiated by the addition of antibodies were quantified by the absorbance change at a wavelength of 680 nm. The initial agglutination rates of the particles covered with smaller antigens were lower. This effect of the molecular size of antigens was larger in P(S/MAA), because small antigens are probably buried in the hydrous polymethacrylic acid layer on the surface of particles. Thus, both the molecular size of antigens and the surface properties of particles affect the sensitivity of the immunological agglutination. On the other hand, the dependence of the initial rate of the immunological agglutination on the ionic strength and pH was similar irrespective of antigen-particle systems. The initial agglutination rates were largest at an ionic strength of approximately 0.05 at pH 7.0 and decreased with increasing pH. This dependence of the sensitivity on the pH and ionic strength is attributed to the electrostatic interactions of particle-particle and antibody-particle.
研究了抗原和颗粒的性质对抗抗原乳胶颗粒免疫凝集动力学的影响。将马细胞色素c、鸡蛋清溶菌酶（HEL）、牛血清白蛋白（BSA）和曲霉属葡萄糖氧化酶物理吸附到苯乙烯-甲基丙烯酸（MAA）共聚物（P（S/MAA））和聚苯乙烯（PS）的无表面活性剂乳胶上。通过680nm波长处的吸光度变化对添加抗体引发的这些蛋白质包被颗粒的免疫凝集初始速率进行定量。被较小抗原覆盖的颗粒的初始凝集速率较低。抗原分子大小的这种影响在P（S/MAA）中更大，因为小抗原可能被埋在颗粒表面的含水聚甲基丙烯酸层中。因此，抗原的分子大小和颗粒的表面性质都会影响免疫凝集的灵敏度。另一方面，无论抗原-颗粒系统如何，免疫凝集初始速率对离子强度和pH的依赖性都是相似的。在pH 7.0时，离子强度约为0.05时初始凝集速率最大，且随着pH升高而降低。灵敏度对pH和离子强度的这种依赖性归因于颗粒-颗粒和抗体-颗粒之间的静电相互作用。
