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人重组白细胞介素-10在大肠杆菌中的表达纯化与鉴定
THE EXPRESSION AND PURIFICATION OF HUMAN INTERLEUKIN-10 EXPRESSED IN E.COLI
【摘要】 为人白细胞介素-10(hIL-10)的理论研究和临床应用研究提供材料。方法:利用基因工程技术,将hIL-10cDNA克隆在大肠杆菌表达载体中,在大肠杆菌中高效表达含凝血酶识别序列的hIL-10的融合蛋白。表达蛋白经凝酶消化后,可去除MS2细菌蛋白。结果:获得高纯度的非融合型rhIL-10。结论:活性分析表明rhIL-10具有抑制LPS刺激的外周血单个核细胞产生IL-6的能力。
【Abstract】 Objective: In order to provide necessary material for future theory and clinic study of IL-10.Methods: The cDNA of human interleukin-10 (hIL-10) was cloned in E. coli expression vector by genetic engineering technique. MS2-IL-10 fusion protein could be overexpressed in E. coli. The MS2 bacteria protein could be removed by thrombin digestion. Results: Purified hIL-10 was obtained. Conclusion: Bioactivity assay revealed that rhIL-10 could inhibit the exprereion of IL-6 by PBMC induced with LPS.
【关键词】 白细胞介素-10/生物合成;
大肠杆菌;
克隆.分子;
【Key words】 Interleukin 10/biosyn Escherichia coli Cloning; molecular;
【Key words】 Interleukin 10/biosyn Escherichia coli Cloning; molecular;
- 【文献出处】 北京医科大学学报 , 编辑部邮箱 ,1997年06期
- 【分类号】R392
- 【被引频次】2
- 【下载频次】167