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中文摘要：
核糖体蛋白L11（ribosome protein L11）是一种高度保守的蛋白质．为研究真核生物的核糖体蛋白L11的功能，从八肋游仆虫（Euplotes octocarinatus）大核基因组中克隆到核糖体蛋白L11基因，构建了重组表达质粒pGEX-6p1-L11，通过谷胱甘肽-Sepharose 4B亲和层析，纯化了重组融合蛋白GST-L11.Pull down分析显示，八肋游仆虫的核糖体蛋白L11与第一类肽链释放因子eRF1a可以在体外相互作用．这一结果提示，与原核生物一样，低等真核生物的核糖体蛋白L11在肽链终止过程中可能起一定的作用．
英文摘要：
The ribosome protein L11 gene was isolated from the Euplotes octocarinatus macronuclear DNA , and cloned into a plasmid pGEX-6pl-L11. The GST fusion protein with L11 （GST-L11 ） was expressed in E. coli, then purified using glutathion-Sepharose 4B affinity chromatography. GST pull-down analysis showed that the recombinant GST-L11 interacted with the polypeptide chain release factor eRFla of E. octocarinatus. The result suggested that the recombinant ribosomal protein Lll from E. octocarinatus could be functional in translation termination.
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