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口蹄疫病毒结构蛋白VP2-3-1的纯化复性与活性检测
引用本文:李平花,郭建宏,刘在新,谢庆阁.口蹄疫病毒结构蛋白VP2-3-1的纯化复性与活性检测[J].中国兽医科学,2004,34(11):53-56.
作者姓名:李平花  郭建宏  刘在新  谢庆阁
作者单位:中国农业科学院,兰州兽医研究所,甘肃,兰州,730046
基金项目:国家重点基础研究发展规划 ( 973 )项目 (G19990 1 1 90 1 )
摘    要:收集含有口蹄疫病毒结构蛋白VP2 3 1基因的大肠埃希氏菌菌液 ,将其超声破壁 ,用菌体裂解液裂解 ,提取包涵体 ,并用 8mol/L尿素溶解 ,收集上清液 ,用亲和层析法纯化融合蛋白VP2 3 1 ,透析法复性 ,并用间接ELISA检测FMDV阳性血清和阴性血清。结果 ,P/N值大于 2 .1 ,说明纯化复性后的目的蛋白有一定的生物活性

关 键 词:口蹄疫病毒  结构蛋白  纯化  复性  活性检测
文章编号:1000-6419(2004)11-0053-04
修稿时间:2004年8月17日

Purification,refold and activity assay of FMDV structural protein VP2-3-1 expressed in Escherichia coli
LI Ping-hua,GUO Jian-hong,LIU Zai-xin,XIE Qing-ge.Purification,refold and activity assay of FMDV structural protein VP2-3-1 expressed in Escherichia coli[J].Veterinary Science in China,2004,34(11):53-56.
Authors:LI Ping-hua  GUO Jian-hong  LIU Zai-xin  XIE Qing-ge
Abstract:The structural protein VP2-3-1 of foot-and-mouth disease virus was produced in Escherichia coli in the form ofinclusion bodies. After extaction from the E.colicells ,the inclusion bodies were solubilized and denatured in the presence of 8 mol/L urea. The expressed VP2-3-1 fusion protein was (purified) by Ni-NTA His. Bind Resin affinity chromatography and renatured finally bythedialysismethod. The activity of the purified VP2-3-1 was assayed by ELISA with FMDV positive serum and negative (serum). The result revealed that the purified protein VP2-3-1 has certain activities.
Keywords:foot-and-mouth disease virus  structural protein  purification  refold  activity assay
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