伊氏锥虫病原性受体纯化的研究

PURIFICATION OF MURINE RECEPTORS ASSOCIATED WITH PATHOGENESIS OF TRYPANOSOMA EVANSI INFECTION

以伊氏锥虫表膜蛋白做配基辛和层析，从小鼠淋巴细胞、巨噬细胞和肾上皮细胞上分别纯化出了分子量相同的一种蛋白质。该蛋白经ＰＡＧＥ电泳分析，是表观分子量约为１２０．１ｋＤ的单一蛋白质，在ＳＤＳ－ＰＡＧＥ电泳系统中显示为分子量分别是７５．１ｋＤ和３５．６ｋＤ的两种蛋白质，从淋巴细胞上纯化出来的该蛋白质具有免疫球蛋白的抗原性，但来源于肾上皮细胞的物质却无此活性。用淋巴细胞膜上的该受体做阻断试验发现，某一浓度下的该受体不仅不能阻断，反而会促进固定的小鼠细胞与锥虫的粘附结合。

Proteins with equal molecular weight of about 120.1 kD have been purified from murine lymphocytes, macrophages and kidney epithelial cells, by means of affinity chromatography ligated with the surface protein of Trypanosoma evansi. They are composed of two subunits,MW 75.1 kD, 35.6 kD, respectively. As analysed by SDS-PAGE electrophoresis protein purified from lymphocytes could not block the adhesion between T. evansi and mouse cells, however. on the contrary, it improved the reaction. Anti-IgG antibody can recognize the protein from lymphocytes but not that with other origin.