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人微小病毒B19VP1独特区蛋白的表达及纯化 被引量:4

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摘要 目的利用原核表达系统表达人微小病毒B19的VP1独特区蛋白,大量发酵培养细菌后纯化蛋白,为制备VP1蛋白的mAb奠定基础。方法构建重组质粒VP1-PQE30,转化大肠杆菌M15,测序正确后发酵培养、IPTG诱导表达,通过SDS-PAGE及Western blot分析表达产物,表达蛋白经AKTA explorer 100快速纯化系统纯化。结果成功地构建原核表达系统VP1-PQE30-M15,经IPTG诱导发酵培养细菌可大量表达VP1蛋白,纯化后蛋白纯度达95%以上。结论重组表达质粒可表达VP1独特区蛋白,高纯度蛋白对制备VP1mAb及疫苗具有重要意义。
出处 《细胞与分子免疫学杂志》 CAS CSCD 北大核心 2007年第4期372-373,共2页 Chinese Journal of Cellular and Molecular Immunology
基金 国家自然科学基金资助项目(30571948)
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参考文献7

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共引文献55

同被引文献57

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