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原核表达系统中 HPV16 L1蛋白的表达与纯化
引用本文:包广宇,谷鸿喜,林道虹,庄敏,隋丽华,王静. 原核表达系统中 HPV16 L1蛋白的表达与纯化[J]. 生物医学工程学杂志, 2002, 19(2): 280-283
作者姓名:包广宇  谷鸿喜  林道虹  庄敏  隋丽华  王静
作者单位:1. 哈尔滨医科大学,微生物教研室,哈尔滨,150086
2. 黑龙江省肿瘤医院,哈尔滨,150086
摘    要:为了建立HPV16L1蛋白原核表达系统系统的纯化方法,纯化目的蛋白,我们构建了pGEX4T-HPV16L1表达质粒。在大肠杆菌BL21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,HPV16L1蛋白在原核表达系统以不溶性包涵体形式存在,通过本病方法可以获得纯化的HPV16L1蛋白,为HPV16L1的应用研究打下了基础。

关 键 词:原核表达系统 HPV16 L1蛋白 纯化

Expression and Purification of Human Papillomavirus Type16 L1 Protein in a Prokaryotic Expression System
Bao Guangyu Gu Hongxi Lin Daohong Zhuang Min Shui Lihua Wang Jing. Expression and Purification of Human Papillomavirus Type16 L1 Protein in a Prokaryotic Expression System[J]. Journal of biomedical engineering, 2002, 19(2): 280-283
Authors:Bao Guangyu Gu Hongxi Lin Daohong Zhuang Min Shui Lihua Wang Jing
Affiliation:Department of Microbiology, Harbin Medical University, Harbin 150086.
Abstract: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.
Keywords:Human papillomavirous 16 Prokaryotic expression system L1 protein Purification
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