Wnek A P, McClane B A
Biochem Biophys Res Commun. 1983 May 16;112(3):1099-105. doi: 10.1016/0006-291x(83)91731-x.
A protein that binds Clostridium perfringens enterotoxin was extracted with NP-40 from rabbit intestinal brush border membranes. This protein was partially purified by affinity chromatography on enterotoxin-coupled CNBr-activated Sepharose 4B. The molecular weight of this protein was approximately 50,000 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Affinity-purified samples containing this protein specifically inhibited biological activity of the enterotoxin on Vero (African green monkey kidney) cells. These studies suggest that this protein may be involved in the binding of the enterotoxin to rabbit intestinal epithelial cells.
用NP - 40从兔肠刷状缘膜中提取出一种能结合产气荚膜梭菌肠毒素的蛋白质。该蛋白质通过在肠毒素偶联的溴化氰活化琼脂糖4B上进行亲和层析得到部分纯化。通过十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳测定，该蛋白质的分子量约为50,000。含有这种蛋白质的亲和纯化样品能特异性抑制肠毒素对Vero（非洲绿猴肾）细胞的生物活性。这些研究表明，这种蛋白质可能参与肠毒素与兔肠上皮细胞的结合。
