Partial purification and characterization of human gamma (immune) interferon.
Partial purification and characterization of human gamma (immune) interferon.
复制标题
人伽马（免疫）干扰素的部分纯化和表征。
DOI：
10.1073/pnas.78.3.1601
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发表时间：
1981
影响因子：
11.1
通讯作者：
Vilcek,J
中科院分区：
文献类型：
--
作者：
Yip,YK;Pang,RH;Urban,C;Vilcek,J
人γ（免疫）干扰素（IFN-γ）是在淋巴细胞培养物中产生的，用佛波酯（12-O-十四烷酰基佛波13-乙酸酯）和纯化的植物血凝素刺激。物理化学分析表明，人IFN-γ是一种糖蛋白，等电点约为8.6，表观分子量为58，000 +/- 3000。IFN-γ的纯化工艺的开发，包括连续的色谱分离的控制孔玻璃，伴刀豆球蛋白A-Sepharose，和生物凝胶P-200。该纯化过程导致比活性从约10（4）（粗培养液）增加到估计10（7）单位/mg蛋白质，累积回收率约为40%的IFN活性。
Human gamma (immune) interferon (IFN-gamma) was produced in lymphocyte cultures stimulated with a phorbol ester (12-O-tetradecanoylphorbol 13-acetate) and purified phytohemagglutinin. Physicochemical analysis showed that human IFN-gamma is a glycoprotein with an isoelectric point around 8.6 and an apparent molecular weight of 58,000 +/- 3000. A purification process for IFN-gamma was developed consisting of sequential chromatographic separations on controlled-pore glass, concanavalin A-Sepharose, and Bio-Gel P-200. This purification process resulted in an increase in specific activity from about 10(4) (crude culture fluid) to an estimated 10(7) units per mg of protein with a cumulative recovery of about 40% of the IFN activity.