Krempien U, Redmann I, Jungwirth C
J Interferon Res. 1985 Winter;5(1):209-14. doi: 10.1089/jir.1985.5.209.
An improved purification method for chick interferon from the allantoic fluid of embryonated chick eggs is described. Interferon prepurified by perchloric acid treatment, zinc acetate precipitation, and chromatography on SP-Sephadex C-25 was further enriched by column chromatography on zinc chelate. Analysis on sodium dodecylsulfate polyacrylamide gel electrophoresis of the interferon preparation with a specific activity of 8 X 10(5) units/mg protein shows that the major antiviral activity migrated in a broad band in the range of 20-29 kD molecular weight. Several protein bands were stainable with Coomassie blue and silver nitrate in this molecular weight range. Between 80 and 95% of the total protein charged to the gel could be removed from the interferon containing fractions by sodium dodecylsulfate polyacrylamide gel electrophoresis.
本文描述了一种从鸡胚尿囊液中提纯鸡干扰素的改良方法。经高氯酸处理、醋酸锌沉淀及SP - Sephadex C - 25柱层析初步纯化后的干扰素，再经锌螯合柱层析进一步富集。对具有8×10⁵单位/毫克蛋白质比活性的干扰素制剂进行十二烷基硫酸钠聚丙烯酰胺凝胶电泳分析表明，主要抗病毒活性在分子量20 - 29 kD范围内呈宽带迁移。在此分子量范围内有几条蛋白带可被考马斯亮蓝和硝酸银染色。通过十二烷基硫酸钠聚丙烯酰胺凝胶电泳，可从含干扰素的组分中去除加样到凝胶上总蛋白的80%至95%。
