摘要
目的制备高纯度、高比活性重组人IL-6。方法对已建立的重组表达载体pBMhIL-6进行温度诱导表达,包涵体提取洗涤和变性复性处理,复性的重组人IL-6蛋白经SP-FF强阳离子交换柱一步纯化。结果所得目的蛋白纯度>97%,经N末端氨基酸测序确证为hIL-6,其比活性高达4.5×108U/mg。结论本研究的纯化工艺简便易行,所得产品纯度高。
Recombinant human interleukin 6(rhIL-6) was obtained from inclusion body expressed by temperatureinduced pBMhIL6 expression vector using extracting,denaturing and refolding techniques.The rhIL6 was further purified by a single step procedure employing SPFF strong cationexchange chromatography.The purified rhIL6 protein showed to have a sequence of amino acid in Nterminal identical to one announced.The purity of the rhIL6 protein purified in this study was 97% and its specific activity reached to 45×108U/mg,which achieved the highest level among those available so far in publications.The rapidity and high efficiency of our scheme would allow the use of an easy and cheap source of rhIL6 for biological study and for diagnostic and potentially therapeutic purpose.
出处
《中华微生物学和免疫学杂志》
CAS
CSCD
北大核心
1998年第1期47-51,共5页
Chinese Journal of Microbiology and Immunology