Sacks D L, MacDonald A B
J Immunol. 1979 Jan;122(1):136-9.
This report describes the isolation of a type-specific antigen of a serotype A strain of Chlamydia trachomatis. The antigen could be identified in sodium dodecyl sulfate-polyacrylamide electrophoretic (SDS-PAGE) analysis of immunoprecipitates of homologously reacted lysates from Bolton-Hunter 125I-labeled elementary bodies, solubilized by sonication and treatment with Nonidet P40. The electrophoretic pattern of this precipitate revealed a peak of unique mobility that was not reproduced by heterologous or control precipitates. Immunoadsorbtion of test antigen with purified IgG fractions from homologous antisera completely removed this peak, whereas similar adsorbtion wth heterologous IgG had minimal effect. Comparison of this antigen in SDS-PAGE with protein standards revealed an approximate m.w. of 27,000.
本报告描述了沙眼衣原体A血清型菌株一种型特异性抗原的分离。该抗原可在对博尔顿-亨特125I标记的原体的同源反应裂解物进行免疫沉淀的十二烷基硫酸钠-聚丙烯酰胺电泳(SDS-PAGE)分析中得以鉴定,这些裂解物经超声处理并用聚山梨醇酯P40处理后溶解。该沉淀物的电泳图谱显示出一个具有独特迁移率的峰,而异源或对照沉淀物均未重现此峰。用来自同源抗血清的纯化IgG组分对测试抗原进行免疫吸附可完全消除此峰,而异源IgG的类似吸附作用则微乎其微。在SDS-PAGE中将该抗原与蛋白质标准品进行比较,结果显示其分子量约为27,000。