卵黄IgG的分离纯化和某些特性的观察ISOLATION,PURIFICATION AND CHARACTERIZATION OF EGG YOLK IgG(EyIgG)
凌天冀;唐俊杰;张丽君;王和;
Ling Tianyi Dep of Microbiol
摘要(Abstract)：
本文报导从免疫母鸡的鸡蛋黄中分离纯化特异性 IgG 的方法。与兔抗鸡全血清作免疫电泳表明,粗制卵黄 IgG(EyIgG)除含 IgG 外尚含少许卵白蛋白,经 DEAE-纤维素层析后,即得较纯的 IgG。每个卵黄约收获粗 EyIgG78～87mg(回收率25.5%),约收纯 IgG27mg(回收率32.3%)。EyIgG 不与人外周血淋巴细胞表面 IgGFc 受体结合,也不结合 SPA,不固定小鼠和人的补体,其出现晚于血清抗体,最高抗体滴度可与血清抗体滴度相比,但维持时间不等。
In this paper,we reported a method for isolation and purification of EyIgG from the eggs laid by immunized hens and characterized some biological properti- es of these proteins.The crude EyIgG can be isolated by precipitating with 33% suturated ammonium sulphate from delipoprotein yolk solutions,while the furth- er purified lgG can be obtained by DEAE-cellulose chromatography.The recovery of both preparations is about 86mg and 27mg per egg respectively,The EyIgG fails to bind lgG Fc receptor on human lymphocytes and SPA,and is incapable of fixing of complement either human or guinea pigs.The yolk antibodies appear later than the serum antibodies,but the highest titer is comparable with the titer of serum in the same chicken,and canmaintain fora long period.
关键词(KeyWords)：
卵黄 IgG;Fc 受体;补体激活作用;葡萄球菌 A 蛋白;免疫电泳
Egg yolk IgG Receptors,Fe Complement activation Staphylococous protein A(SPA)Immunoeletrophooesis
基金项目(Foundation):
作者(Author):
凌天冀;唐俊杰;张丽君;王和;
Ling Tianyi Dep of Microbiol
Email:
DOI: 10.19367/j.cnki.1000-2707.1987.04.003
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