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表达重组人骨形态发生蛋白-7工程菌的发酵及表达产物的纯化
引用本文:王国栋,王世立,韩金祥,张翠,张更林,车婧.表达重组人骨形态发生蛋白-7工程菌的发酵及表达产物的纯化[J].生物技术通讯,2006,17(3):345-348.
作者姓名:王国栋  王世立  韩金祥  张翠  张更林  车婧
作者单位:山东省医药生物技术研究中心,卫生部生物技术药物重点实验室,山东,济南,250062
基金项目:国家高技术研究发展计划项目(2003AA2Z3532)
摘    要:目的:研究表达重组人骨形态发生蛋白-7工程菌的发酵和表达产物的纯化工艺。方法:利用16L发酵罐发酵培养工程菌,设定了溶氧、搅拌速度、诱导时机、补料和培养基pH值等发酵条件;通过包涵体洗涤、离子交换层析法纯化目的蛋白。结果:工程菌目的蛋白质表达量占菌体总蛋白质的30%以上,纯化后目的蛋白的纯度可达98%。结论:建立了大肠杆菌高效表达人骨形态发生蛋白-7的发酵及纯化工艺。

关 键 词:人骨形态发生蛋白-7  发酵  纯化  大肠杆菌
文章编号:1009-0002(2006)03-0345-04
收稿时间:2005-09-16
修稿时间:2005年9月16日

Fermentation of Recombinant Escherichia coli Strain Expressing Human Bone Morphogenetic Protein-7(hBMP-7) and Purification Procedure of rhBMP-7
WANG Guo-dong,WANG Shi-li,HAN Jin-xiang,ZHANG Cui,ZHANG Geng-lin,CHE Jing.Fermentation of Recombinant Escherichia coli Strain Expressing Human Bone Morphogenetic Protein-7(hBMP-7) and Purification Procedure of rhBMP-7[J].Letters in Biotechnology,2006,17(3):345-348.
Authors:WANG Guo-dong  WANG Shi-li  HAN Jin-xiang  ZHANG Cui  ZHANG Geng-lin  CHE Jing
Abstract:Objective:To study the fermentation and purification of recombinant human bone morphogenetic protein(rhBMP-7).Methods:Dissolving oxygen,stirring velocity,induction condition,nutrition and pH of medium were investigated by using 16 L fermentor.After the washing of the inclusion body,the recombinant protein purified efficiently was solubilized in urea through ion-exchange chromatiography.Results:Expression quantity of recombinant protein was above 30% of total bacteria protein.The recombinant protein reached the purity of 98% after purification.Conclusion:Fermentation condition and purification techniques for rhBMP-7 which was high expressed in Escherichia coli were established.
Keywords:human bone morphogenetic protein  fermentation  purification  Escherichia coli
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