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克隆伊氏锥虫2个VSG的分离纯化和电泳分析
引用本文:周金林,沈杰,周勇志. 克隆伊氏锥虫2个VSG的分离纯化和电泳分析[J]. 中国兽医学报, 1999, 19(3): 267-269
作者姓名:周金林  沈杰  周勇志
作者单位:中国农科院上海家畜寄生虫病研究所,上海,200232
摘    要:用蛋白酶抑制剂TLCK对伊氏锥虫安徽株单虫克隆的2个抗原变异体ShTat1.3和ShTat1.5的变异表面糖蛋白(VSG)进行了分离纯化,采用SDS-PAGE和等电聚焦电泳对VSG的分子量和等电点进行比较研究。结果,VSG的分子量约为40000,等电点约为pH5.0,但2个抗原变异体的VSG在分子量和等电点都有差异,提示其抗原变异由VSG变化引起。

关 键 词:伊氏锥虫  变异表面糖蛋白  分离纯化  电泳分析
修稿时间:1998-07-13

Isolation and Electrophoresis Analysis on Two VSG of a Cloned Trypanosoma evansi
Zhou Jinlin,Shen Jie,Zhou Yongzhi. Isolation and Electrophoresis Analysis on Two VSG of a Cloned Trypanosoma evansi[J]. Chinese Journal of Veterinary Science, 1999, 19(3): 267-269
Authors:Zhou Jinlin  Shen Jie  Zhou Yongzhi
Abstract:Two VSG of T evansi were isolated and purificated by applying proteolytic enzyme inhititor TLCK. Molecular weight of VSG is about 40 000 measured by SDSPAGE and isoelectric point about pH5.0 by isoelectrofocusing. VSG of ShTat1.3 and ShTat1.5 were difference either in molecular weight or in isoelectric point. The results prove antigenic variation of T evansi is caused by change of VSG.
Keywords:Trypanosoma evansi  VSG  isolation and purification  electrophoresis  
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