| 乳腺珠蛋白基因在大肠杆菌中的诱导表达及纯化研究 |
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| 引用本文： | 刘秀娜,王仙园,周娟,潘自铁,赵力军,胡川闽. 乳腺珠蛋白基因在大肠杆菌中的诱导表达及纯化研究[J]. 解放军护理杂志, 2005, 22(11): 7-9,44 |
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| 作者姓名： | 刘秀娜 王仙园 周娟 潘自铁 赵力军 胡川闽 |
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| 作者单位： | 第三军医大学,护理管理学教研室;第三军医大学,临床生化教研室,重庆,400038;National Center for HIV, STD and TB Prevention,Centers for Disease Control and Prevention.1600 Clifton Road, Atalanta, GA30333, USA |
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| 基金项目： | 重庆市科委应用基础研究资助项目（2004）、校归国人员启动资金资助（2004） |
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| 摘 要： | 目的 克隆乳腺珠蛋白（human mammaglobin，hMAM）编码全长cDNA，原核表达并纯化蛋白产物，为后期研制乳腺癌早期诊断试剂盒奠定基础，从而为早期发现乳腺癌提供科学的监测方法。方法 自乳腺癌组织提取总RNA，通过RT-PCR克隆hMAMcDNA，构建pQFA0-hMAM表达质粒，在大肠杆菌M15中表达，利用镍-亚硝胺乙酸组氨酸（Ni-NTA-His）亲和层析法对重组蛋白进行纯化。结果 表达的融合蛋白以不溶性包涵体形式存在，纯化后得到纯度为97％的目的蛋白。结论 成功地纯化出hMAM重组蛋白。
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| 关 键 词： | 乳腺癌 人乳腺珠蛋白 原核表达系统 蛋白纯化 |
| 文章编号： | 1008-9993（2005）11-0007-04 |
| 收稿时间： | 2005-04-10 |
| 修稿时间： | 2005-09-11 |
Prokaryotic Expression and Purification of Human Mammaglobin Gene in E. coli |
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| LIU Xiu-na,WANG Xian-yuan,ZHOU Juan,PAN Zi-tie,ZHAO Li-jun,HU Chuan-min. Prokaryotic Expression and Purification of Human Mammaglobin Gene in E. coli[J]. Nursing Journal of Chinese People's Liberation Army, 2005, 22(11): 7-9,44 |
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| Authors: | LIU Xiu-na WANG Xian-yuan ZHOU Juan PAN Zi-tie ZHAO Li-jun HU Chuan-min |
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| Abstract: | Objective To clone the cDNA in full-length of human mammaglobin(hMAM) and to do prokaryotic expression and purify hMAM protein,in order to provide an experimental basis for early diagnostic reagent bottle and early screening of breast cancer.Methods hMAM cDNA was amplified through RT-PCR from breast cancer tissue.The recombination pQE40-hMAM vector was constructed and expressed in E.coli M15 after induction by IPTG.The fusion protein was purified with Ni-NTA-His affinity chromatography.Results The fusion protein formed inclusion body in prokaryotic expression system and the renatured protein was purified with purity of 97%.Conclusion The recombinant hMAM is successfully purified. |
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| Keywords: | breast cancer human mammaglobin prokaryotic expression system protein purification |
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