Felsted R L, Leavitt R D, Bachur N R
Biochim Biophys Acta. 1975 Sep 9;405(1):72-81. doi: 10.1016/0005-2795(75)90316-5.
Half-gram quantities of phytohemagglutinin lectins are purified from saline extracts of red kidney beans (Phaseolus vulgaris) by affinity absorption on porcine thyroglobulin-Sepharose. All of the mitogenic and erythroagglutinin activity of the saline extract is removed by this absorbent, and 74% of the original erythroagglutinating activity elutes from the affinity absorbent representing a 25-fold purification. Five distinct proteins appear in the polyacrylamide gel electrophoresis of the affinity absorbent eluate. Although all five proteins specifically bind to porcine thyroglobulin, the cathodal migrating proteins bind more strongly than the anodal migrating proteins. The most cathodal proteins are potent erythroagglutinins. This simple, efficient method is used to prepare all the active components of the phytohemagglutinin family in large yield and high purity.
通过在猪甲状腺球蛋白-琼脂糖凝胶上进行亲和吸附，从红芸豆（菜豆）的盐提取物中纯化出半克量的植物血凝素凝集素。这种吸附剂去除了盐提取物的所有促有丝分裂和红细胞凝集活性，74%的原始红细胞凝集活性从亲和吸附剂上洗脱下来，纯化倍数为25倍。亲和吸附剂洗脱液的聚丙烯酰胺凝胶电泳中出现了五种不同的蛋白质。尽管所有五种蛋白质都能特异性结合猪甲状腺球蛋白，但向阴极迁移的蛋白质比向阳极迁移的蛋白质结合更强。最向阴极的蛋白质是强效红细胞凝集素。这种简单、高效的方法用于大量制备高纯度的植物血凝素家族的所有活性成分。
