Hassl A, Aspöck H, Flamm H
Abteilung für Medizinische Parasitologie, Universität Wien.
Zentralbl Bakteriol Mikrobiol Hyg A. 1987 Dec;267(2):247-53. doi: 10.1016/s0176-6724(87)80009-3.
Eggs from immunized hens were used as a source of yolk antibodies directed against soluble proteins of Toxoplasma gondii. The yolk immunoglobulins (IgY) were extracted and purified by the use of three different methods. The antibody yield and the purity of each batch were determined by protein measurements, gel filtration and isoelectric focusing. A sequence of two precipitation steps, i.e. a precipitation by polyethylene glycol followed by an alcohol treatment, was shown to be the most effective purification method. The specificity of the yolk antibodies was evaluated by means of an indirect hemagglutination assay, an immunodiffusion test and an immunoelectrophoresis. It was compared with the specificity of IgG antibodies obtained from sera hyperimmunized rabbits. The precipitation patterns of IgY and IgG antibodies were non-identical. This results indicates differences between the specificities of egg yolk IgY antibodies and rabbit IgG serum antibodies, although both animal species had been immunized with identical antigen preparations.
来自免疫母鸡的鸡蛋被用作针对刚地弓形虫可溶性蛋白的卵黄抗体来源。通过三种不同方法提取并纯化卵黄免疫球蛋白(IgY)。通过蛋白质测定、凝胶过滤和等电聚焦确定每一批次的抗体产量和纯度。结果表明,由聚乙二醇沉淀后再进行酒精处理的两步沉淀法是最有效的纯化方法。通过间接血凝试验、免疫扩散试验和免疫电泳评估卵黄抗体的特异性。并将其与从超免疫兔血清中获得的IgG抗体的特异性进行比较。IgY和IgG抗体的沉淀模式并不相同。这一结果表明,尽管两种动物都用相同的抗体制剂进行了免疫,但卵黄IgY抗体和兔IgG血清抗体的特异性存在差异。