摘要
目的 :探讨人乳头瘤病毒 16型主要衣壳蛋白 L 1的纯化方法。方法 :分别利用亲和层析和离子交换层析对重组融合蛋白 p ET30 a- 6× His- L 1进行了纯化。结果 :以包涵体形式表达的重组蛋白在变性条件下经 Ni- NTA Agarose、Q- Sepharose FF纯化 ,透析复性后均获得较高纯度 ,回收率分别为 30 %和2 9%。结论 :亲和层析和离子交换层析都是纯化重组 L 1蛋白的适宜方法 ,二者纯化效率相当。
Objective:To study the methods of purification of HPV16 L1 protein ha expressed in Escherichia coli BL21 with the expression vector pET30a.Methods:In this study,affinity chromatography and ion exchange chromatography are used to purify recombinant fussion protein pET30a 6×His L1.Results:High purity of the recombinant proteins which expressed in the form of insoluble inclusion bodies have been obtained after denaturation,purification and renaturation.Purify yield are 30% and 29% individually.Conclusion:Affinity chromatography and ion exchange chromatography are both efficient methods to purify recombinant L1 protein.
出处
《承德医学院学报》
2002年第2期85-87,共3页
Journal of Chengde Medical University
