DEAE-Sepharose阴离子交换柱一步纯化重组人IL-6

Single-step purification of recombinant human interleukin-6 employing DEAE-Seph-arose weak anionic-exchange chromatography

目的：为了制备高纯度、高活性的重组人白细胞介素与。方法：化学诱导重组表达载体pT7．7hIL-6进行蛋白表达，菌体经超声破碎分离包涵体，并对包涵体进行洗涤、变性和复性处理，用DEAE-Sepharose CL-6B弱阴离子交换柱一步纯化复性的重组人IL-6。采用3H-TdR法测定rh-IL-6的活性。结果：表达产物经纯化后纯度达95％，比活性为3．0x10^8U/mg。结论：本实验设计的纯化工艺简便易行，所得产品纯度度、产率高。

Abstract Objective: To prepare high-purification and high-specific activity of recombinant human interleukin-6 (rhIL-6). Methods: The rhIL-6 was obstained from inclusion body expressed by IPTG-induced pT7.7hIL-6 expressed vector using extracting,denature and refolding techniques. The rhTL-6 was further purified by anionic-exchange chromatography. Activity of rhIL-6 was measured by 3H-TdR method. Results: After a single-step purification,the product purity reach 95% and it's specific activity was 3.0 x 10~8 U/mg. Conclusion:This scheme of puri-fication was an easy way requiring rhTL-6.