免疫亲和层析法纯化棕尾别麻蝇(Sarcophagaperegrina)幼虫血淋巴凝集素

 报道了利用免疫亲和层析法纯化棕尾别麻蝇幼虫血淋巴凝集素的结果．哺乳动物红细胞能够特异地吸附凝集素．用兔红细胞与麻蝇幼虫血淋巴凝集素形成的复合体免疫供血家兔，得到麻蝇幼虫血淋巴凝集素的抗体．再利用抗体制备亲和吸附柱，通过免疫亲和层析一次性纯化了麻蝇幼虫血淋巴凝集素． Ｓ Ｄ Ｓ Ｐ Ａ Ｇ Ｅ结果显示，该凝集素的分子量约为７３ ｋ Ｄ．这一结果，与用对麻蝇幼虫血淋巴凝集素有抑制作用的糖蛋白—胎球蛋白和甲状腺球蛋白为配基，亲和层析纯化的结果完全相同，表明用这种免疫亲和层析法纯化凝集素是可行的．为不清楚专一性识别糖或专一性识别糖不典型，难于用普通亲和层析纯化的凝集素，提供了一种有效的纯化方法．

Purification of Lectin in Hemolymph of Sarcophaga peregrina Larvae by Immuno affinity Chromatography

A method of immuno affinity chromatography for insect lectin purification was described.Antibody against lectin in the hemolymoph of Sarcophaga peregrina larvae was raised by immunizing male rabbits and the complex of lectin binding with to rabbit blood red cells was used as antigen.Then the antibody used as immuno affinity ligand was coupled onto the matrix Sepharose 4B.The lectin with M r 73 kD in the hemolymph of S.peregrina larvae was purified through immuno affinity chromatography.The purified lectin was shown the same molecular weight as that purified from general affinity chromatography by using two glycoproteins as affinity ligands,which could inhibit the activity of this lectin.Comparison of these three methods indicated that the way of this immuno affinity chromatography did work well in purification of lectins.Immuno affinity chromatography would be an effective and an alternative way for insect lectin purification,especially when the specific binding saccharides of the lectins were unknown or atypical.