原核表达系统中HPV16L1蛋白的表达与纯化

Expression and Purification of Human Papillomavirus Type16 L1Protein in a Prokaryotic Expression System

为了建立 HPV16 L1蛋白原核表达系统的纯化方法 ,纯化目的蛋白 ,我们构建了 p GEX4 T- HPV16 L1表达质粒。在大肠杆菌 BL2 1表达系统中表达 ,经过包涵体提取 ,8M尿素溶解 ,分级透析除去尿素 ,亲和层析进行提纯。结果显示 ,HPV16 L1蛋白在原核表达系统以不溶性包涵体形式存在 ,通过本方法可以获得纯化的 HPV16 L1蛋白 ,为 HPV16

This study was intended to establish a method of purification of HPV16 L1 protein expressed in a prokaryotic system and to obtain the purified protein. The prokaryotic expression vector pGEX 4T 1 HPV16 L1 was constructed and transformed into E.coli BL21 cell, and induced by 1mM IPTG to express HPV16L1 protein. The inclusion bodies were isolated and solubilized with 8M urea. After the urea was removed by gradual dialysis, the denatured L1 protein were renatured and then were purified by affinity chromatography. The results showed that HPV16L1 protein formed inclusion bodies in bacterial expression system,suggesting that this assay can be used to purify HPV16L1 protein and hence provide a basis for studying the applications of HPV16 L1 protein.