目的：研究人ＩＬ６基因在大肠杆菌中的高效表达及表达产物的纯化。方法：采用ＲＴ－ＰＣＲ方法克隆了人ＩＬ６ｃＤＮＡ，用ｐＢＶ２２０载体对ＩＬ６基因进行了表达调控研究，用阴离子交换柱和凝胶柱对表达产物进行纯化，用ＭＴＴ法测定ｒｈＩＬ６的活性。结果：表达调控研究发现，当ＳＤ序列到ＡＴＧ之间的距离为６ｂｐ和１０ｂｐ时在ＳＤＳ－ＰＡＧＥ胶上未见明显表达，而当距离为５ｂｐ、７ｂｐ、８ｂｐ、９ｂｐ时均可获高效表达，最高表达量占菌体总蛋白的２６％。表达产物经变性复性及纯化后产品纯度达９８％，比活性为１１×１０８Ｕ／ｍｇ。结论：本研究为ｒｈＩＬ６的中试生产奠定了坚实的基础 Objective: To study the high expression of human IL6 gene in Escherichia coli and the purification of expression product. Methods: Human IL-6 cDNA was cloned by RT-PCR and the expression of IL-6 gene was regulated by pBV220 vector. The expressed product was purified by anion exchange column and gel column. The expression of rhIL-6 active. Results: The regulation of expression showed no significant expression on SDS-PAGE gels when the distance between SD sequence and ATG was 6 bp and 10 bp, and was highly expressed when the distance was 5 bp, 7 bp, 8 bp and 9 bp, The highest expression accounted for 26% of the total bacterial protein. After denaturation and purification of the expressed product, the purity of the product reached 98%, and the specific activity was 1 × 108U / mg. Conclusion: This study lays a solid foundation for the pilot-scale production of rhIL-6