Tarkhanova I A, Sycheva I M, Tolovskaia K R, Kul'berg A Ia
Zh Mikrobiol Epidemiol Immunobiol. 1979 Jun(6):27-31.
In a comparative study the affinity of rabbit and human IgG, native, reduced and aggregated by various methods, to protein A obtained from the cell wall of Staphylococcus aureus was determined. For this purpose the method of the passive hemagglutination inhibition test was developed. The affinity to protein A was found to grow considerably after specific or non-specific IgG aggregation and to decrease by 60% after local damage affecting the structure of the IgG molecule waist as a result of the dissolution of the disulfide bond between its heavy chains. The problem of similarity between such effector properties of IgG as its ability to activate the complement system and to combine with protein A is considered, as well as the problem of the pathogenetic role of immune complexes bound with protein A.
在一项比较研究中,测定了天然、经还原以及通过各种方法聚集的兔和人IgG对从金黄色葡萄球菌细胞壁获得的蛋白A的亲和力。为此开发了被动血凝抑制试验方法。发现特异性或非特异性IgG聚集后,其对蛋白A的亲和力显著增加;而由于IgG分子腰部重链间二硫键溶解导致其结构局部受损后,亲和力降低60%。文中还探讨了IgG激活补体系统和与蛋白A结合等效应特性之间的相似性问题,以及与蛋白A结合的免疫复合物的致病作用问题。