【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，并且是目前已报道的重组人ＩＬ－６蛋白中比活性最高者更多还原

【Abstract】 Recombinant human interleukin 6(rhIL-6) was obtained from inclusion body expressed by temperatureinduced pBMhIL6 expression vector using extracting,denaturing and refolding techniques.The rhIL6 was further purified by a single step procedure employing SPFF strong cationexchange chromatography.The purified rhIL6 protein showed to have a sequence of amino acid in Nterminal identical to one announced.The purity of the rhIL6 protein purified in this study was 97% and its specific activity reached to 45×108U/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 rhIL6 for biological study and for diagnostic and potentially therapeutic purpose.更多还原