Tixier G, Alouf J E
Ann Microbiol (Paris). 1976 Nov-Dec;127B(4):509-24.
Delta toxin, a hemolytic exocellular protein excreted by C. perfringens type C has been purified to homogeneity, assessed by polyacrylamide disc gel electrophoresis. Purification steps involved successively calcium phosphate gel formation in culture supernatant fluid, salting-out of unadsorbed material by ammonium sulfate to 50 % saturation, isoelectric focusing and gel filtration on Sephadex G75. Purified toxin appears as a basic protein occuring in two forms with isoelectric points of 8.8 and 9.4 as disclosed by isoelectric focusing. Molecular weight estimated by SDS-polyacrylamide disc gel electrophoresis was found to be close to 42,000 for the two forms. The lytic activity of delta toxin is inhibited by Ca++ and EDTA. The toxin is activated by short-term treatment with low concentration of trypsin.
δ毒素是由C型产气荚膜梭菌分泌的一种溶血细胞外蛋白，已通过聚丙烯酰胺圆盘凝胶电泳评估其纯度至均一性。纯化步骤依次包括在培养上清液中形成磷酸钙凝胶、用硫酸铵将未吸附物质盐析至50%饱和度、等电聚焦以及在葡聚糖凝胶G75上进行凝胶过滤。经等电聚焦显示，纯化后的毒素表现为一种碱性蛋白，有两种形式，其等电点分别为8.8和9.4。通过SDS - 聚丙烯酰胺圆盘凝胶电泳估计，这两种形式的分子量均接近42,000。δ毒素的溶血活性受到Ca++和EDTA的抑制。该毒素经低浓度胰蛋白酶短期处理后被激活。
