| 血小板生成素突变体的克隆和扩增及其融合蛋白在大肠杆菌中… |
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| 引用本文： | 田生礼 刘丽. 血小板生成素突变体的克隆和扩增及其融合蛋白在大肠杆菌中…[J]. 中华血液学杂志, 1997, 18(12): 634-637 |
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| 作者姓名： | 田生礼 刘丽 |
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| 摘 要： | 目的：通过获得编码血小板生成素成熟肽Ｎ端１￣１９６个氨基酸的突变体ｃＤＮＡ在大肠杆菌ＪＭ１０９中的表达，为Ｔｐｏ进一步的结构和功能研究提供材料来源。方法：用多聚酶链反应及ＤＮＡ重组技术，将ＰＣＲ产物克隆到ｐＵＣ１９载体并测序，然后克隆到表达载体ｐＭＡｌ－ｃ２上。
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| 关 键 词： | 血小板生成素 突变体 融合蛋白 基因表达 |
High expression of human thrombopoietin mutant fusion protein in E. coli] |
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| S Tian,L Liu,B Feng. High expression of human thrombopoietin mutant fusion protein in E. coli][J]. Chinese Journal of Hematology, 1997, 18(12): 634-637 |
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| Authors: | S Tian L Liu B Feng |
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| Affiliation: | Norman Bethune University of Medical Sciences, Changchun 130021. |
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| Abstract: | OBJECTIVE: To obtain human thrombopoietin (Tpo)mutant cDNA encoding mature peptide N terminal 1 approximately 196 amino acids and investigate its expression in E. coli JM109. METHODS: Polymerase chain reaction and DNA recombination techniques were employed. PCR product was inserted into pUC19 vector and sequenced and then cloned into expression vector pMAL-c2. RESULTS: E. coli JM109 cells with plasmid pMAL -MBP/TpoM were induced by IPTG for 4-5 hours. SDS-PAGE analysis showed that MBP/TpoM molecular weight is about 63KD. Scanning analysis indicated that expressed protein accounts up to 37% of total E. coli proteins. CONCLUSION: The Tpo mutant of interest is successfully expressed in E. coli JM109 cells. |
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