Schwartzman J D, Krug E C
Department of Pathology, University of Virginia School of Medicine, Charlottesville 22908.
Exp Parasitol. 1989 Jan;68(1):74-82. doi: 10.1016/0014-4894(89)90010-6.
We have previously reported on a series of monoclonal antibodies that recognize the rhoptries of Toxoplasma gondii and that interfere with the action of penetration enhancing factor. The antibodies immunoprecipitate several related antigens from [35S]methionine-labeled parasites that range in size from 60 to 43 kDa. By immunoblot, one of the antibodies reacts with the 60 kDa protein in the presence of protease inhibitors. Trypsin digestion of the antigen destroyed antigenic reactivity indicating that the 60 kDa antigen is a protein. The antigen was stable to periodate oxidation and failed to react with Schiff's reagent, indicating that the antigen contains little or no carbohydrate. Two-dimensional gel electrophoresis followed by immunoblot showed that the antigen recognized by Tg 49 was an acidic protein with an approximate pI of 5.8.
我们之前报道过一系列单克隆抗体,这些抗体可识别刚地弓形虫的棒状体,并干扰穿透增强因子的作用。这些抗体从[35S]甲硫氨酸标记的寄生虫中免疫沉淀出几种相关抗原,其大小范围为60至43 kDa。通过免疫印迹法,其中一种抗体在蛋白酶抑制剂存在的情况下与60 kDa蛋白发生反应。抗原经胰蛋白酶消化后破坏了抗原反应性,表明60 kDa抗原是一种蛋白质。该抗原对高碘酸盐氧化稳定,且不与席夫试剂反应,表明该抗原几乎不含或不含碳水化合物。二维凝胶电泳后进行免疫印迹显示,Tg 49识别的抗原是一种酸性蛋白,其近似等电点为5.8。