Bridgen P J, Anfinsen C B, Corley L, Bose S, Zoon K C, Rüegg U T, Buckler C E
J Biol Chem. 1977 Oct 10;252(19):6585-7.
Human lymphoblastoid interferon was produced on an 800-liter scale (2.6 X 10(9) units) by induction of Namalva cells with Newcastle disease virus, strain B1. The interferon was partially purified by anti-leukocyte interferon affinity chromatography, sulfopropyl Sephadex ion exchange chromatography, isoelectric focusing, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Recovery of interferon after gel electrophoresis varied from 11 to 33% based on the original crude material, with about 35,000-fold purification. The gel electrophoresis resolved the antiviral activity into two components with apparent molecular weights of 18,000 and 22,000; treatment with glycosidases resulted in all the activity being associated with the lower molecular weight species. Interferon activity could be completely (85 to 113%) recovered from the gels by elution into a buffer containing sodium dodecyl sulfate. The presence of sodium dodecyl sulfate did not appear to affect the assay of interferon. The protein could also be completely (75 to 106%) eluted from gels stained with coomassie blue, again with no loss in activity.
人淋巴母细胞干扰素通过用新城疫病毒B1株诱导纳马瓦细胞，以800升规模（2.6×10⁹单位）生产。干扰素通过抗白细胞干扰素亲和层析、磺丙基葡聚糖离子交换层析、等电聚焦和十二烷基硫酸钠-聚丙烯酰胺凝胶电泳进行部分纯化。基于原始粗品，凝胶电泳后干扰素的回收率为11%至33%，纯化倍数约为35000倍。凝胶电泳将抗病毒活性分离为两个组分，表观分子量分别为18000和22000；用糖苷酶处理导致所有活性与较低分子量的组分相关。通过洗脱到含有十二烷基硫酸钠的缓冲液中，可从凝胶中完全（85%至113%）回收干扰素活性。十二烷基硫酸钠的存在似乎不影响干扰素的测定。该蛋白质也可从考马斯亮蓝染色的凝胶中完全（75%至106%）洗脱，且活性无损失。
