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我们曾报道过猪外周血淋巴细胞E受体(GP_1)与人的E受体在血清学上具有交叉反应性。本文报告将兔杭GP_1 IgG与溴化氰活化的Sepharose 4B偶联,制备免疫吸附柱,然后从猪外周血淋巴细胞表面,猪血淸和正常人血清中分离E受体,以及E受体理化性质研究的初步结果。测定E受体体外生物活性的反向E-玫瑰花试验结果表明,这样分离得到的三种不同来源的E受体在体外均具有抑制猪外周血淋巴细胞与绵羊红细胞形成E-玫瑰花活性。以Pharmacia低分子量标准蛋白混合物(分子量范围:14,400～94,000 Daltons)作标准进行SOS-聚丙烯酰胺凝胶电泳测定E受体的分子量为58,000;聚丙烯酰胺凝胶聚焦电泳测定其等电点为6.8左右。这些实验结果表明,用亲和层析法分离得到的E受体与前文报道的即自猪淋巴细胞表面直接提纯 的GP_1在化学,免疫学和生物学性质方面完全一致。同时证明E受体不仅存在于淋巴细胞表面,而且游离存在于血淸中。 以绵羊、家兎和大鼠等已知共淋巴细胞在体外不能与未经处理的绵羊红细胞形成E-玫瑰花的动物血淸作对照,经同一免疫吸附柱分离,均可得到能与抗GP_1 IgG结合的蛋白组份。经比较研究发现,该结合蛋白的理化性质——分子量、等电点——和上述E受体基本相同,但反向E-玫瑰花试验结果表明,这些结合蛋白在体外不具有抑制E-
We have previously reported that porcine peripheral blood lymphocyte E receptor (GP_1) is serologically cross-reactive with human E receptor. In this paper, Rabbit Hanging GP_1 IgG was coupled with Sepharose 4B activated by cyanogen bromide to prepare an immunoadsorption column. The E receptor was isolated from the surface of porcine peripheral blood lymphocytes, porcine blood and normal human serum, and the physiology of E receptor Preliminary results of the nature of the study. The results of reverse E-rosette assaying the biological activity of E receptor in vitro showed that the three different derived E receptors isolated in this way can inhibit the formation of E-rose activity in porcine peripheral blood lymphocytes and sheep erythrocytes in vitro. The molecular weight of E receptor was determined to be 58,000 by SOS-polyacrylamide gel electrophoresis using a Pharmacia low molecular weight standard protein mixture (molecular weight range: 14,400 to 94,000 Daltons); its polyacrylamide gel focusing electrophoretic assay showed an isoelectric point of 6.8 about. These experimental results indicate that the E receptor isolated by affinity chromatography is chemically and immunologically and biologically consistent with the previously reported GP_1 directly purified from the surface of porcine lymphocytes. At the same time, it is proved that E receptor not only exists on the surface of lymphocytes, but also exists in the bloodstream. The known co-lymphocytes, such as sheep, clam and rat, can not be compared with untreated sheep erythrocytes to form E-rose blood in vitro, and separated by the same immunosorbent column. IgG-binding protein component. The comparative study found that the physical and chemical properties of the binding protein - molecular weight, isoelectric point - and the E receptor is basically the same, but the reverse E-rose test results show that these binding proteins do not have in vitro inhibition of E-