|
|||||
|
|
| 猪瘟病毒E2重组蛋白纯化和复性条件的研究 | |
| 引用本文： | 胡慧,邱昌庆,张彦明. 猪瘟病毒E2重组蛋白纯化和复性条件的研究[J]. 中国兽医科学, 2005, 35(4): 251-255 |
| 作者姓名： | 胡慧 邱昌庆 张彦明 |
| 作者单位： | 1. 中国农业科学院,兰州兽医研究所,农业部畜禽病毒学重点开放实验室,甘肃,兰州,730046;西北农林科技大学,动物科技学院,陕西,杨凌,712100 2. 中国农业科学院,兰州兽医研究所,农业部畜禽病毒学重点开放实验室,甘肃,兰州,730046 3. 西北农林科技大学,动物科技学院,陕西,杨凌,712100 |
| 基金项目： | 社会公益研究专项资助重点项目(2001DIA10006) |
| 摘 要： | 对猪瘟病毒(CSFV) C株、LT株E2基因主要抗原区在pGEX系列表达载体中原核表达的融合蛋白进行了变性、复性和纯化回收试验。用建立的变性、复性和纯化方法,获得了可溶性的纯化蛋白E2,其纯度达70%,回收率为10%。对复性纯化的E2蛋白进行了免疫活性检测,结果表明,其比未纯化蛋白的免疫活性高20倍左右。 |
| 关 键 词： | 猪瘟病毒 E2重组蛋白 包涵体 复性 纯化 |
| 文章编号： | 1000-6419(2005)04-0251-05 |
| 修稿时间： | 2004-12-31 |
Study on purification and renaturation conditions of recombinant E2 proteins of classical swine fever virus |
|
| HU Hui,QIU Chang-qing,ZHANG Yan-ming. Study on purification and renaturation conditions of recombinant E2 proteins of classical swine fever virus[J]. Chinese Veterinary Science, 2005, 35(4): 251-255 | |
| Authors: | HU Hui QIU Chang-qing ZHANG Yan-ming |
| Abstract: | The fusion recombinant proteins of CSFV strain C and LT, which had been expressed with vector pGEX in Escherichia coli, were denatured, renatured and extracted experimentally. The results showed that the obtained E2 proteins were dissolvable and active, and their purification rate and the reco- very rate reached 70% and 10% respectively. Immunological activity of the renatured and purified E2 proteins was 20 times higher than the unpurified ones. |
| Keywords: | classical swine fever virus recombinant E2 protein inclusion body renaturation purification |
| 本文献已被 CNKI 万方数据 等数据库收录！ | |