在特异性纯化的免疫吸附剂上纯化小鼠干扰素。
Purification of mouse interferon on specifically purified immunoadsorbent.
作者信息
Hajnicka V, Fuchsberger N, Borecký L
出版信息
Arch Immunol Ther Exp (Warsz). 1977;25(5):619-22.
A one-step purification procedure using affinity chromatography on purified anti-interferon antibodies makes possible to obtain highly purified interferon preparations. Antibodies against purified mouse fibroblast interferon were covalently bound to activated CNBr-Sepharose 4B. This immunoadsorbent had a binding capacity of 125,800 mouse fibroblast interferon units per 4.8 ml of gel. The binding capacity for mouse leukocytes was similar while for serum interferon it was lower. When analyzed in polyacrylamide gel, the electrophoretic profiles of purified IF had a similar shape to that of unpurified IF. The results of this purification procedure are not influenced by volume, biological activity and/or purity of the starting material.
使用纯化的抗干扰素抗体进行亲和层析的一步纯化程序能够获得高度纯化的干扰素制剂。针对纯化的小鼠成纤维细胞干扰素的抗体被共价结合到活化的溴化氰-琼脂糖4B上。这种免疫吸附剂每4.8毫升凝胶具有125,800个小鼠成纤维细胞干扰素单位的结合能力。对小鼠白细胞的结合能力相似，而对血清干扰素的结合能力较低。在聚丙烯酰胺凝胶中分析时，纯化后的干扰素的电泳图谱与未纯化的干扰素具有相似的形状。该纯化程序的结果不受起始材料的体积、生物活性和/或纯度的影响。
Zotero 插件