%0 Journal Article
%T Strong Expression of Recombinant Human Morphogenetic Protein-4 in Escherichia coli and its Bioassay in vivo<br>大肠杆菌中高效表达rhBMP-4的探讨及初步活性测定
%A GAO Si-hong
%A WANG Ju
%A DONG Que-wei
%A LIU Kan
%A LIU Xue-ting
%A HONG An
%A XIE Qiu-ling
%A SUN Fen-yong
%A <br>高思红
%A 汪炬
%A 董群伟
%A 刘侃
%A 刘雪婷
%A 洪岸
%A 谢秋玲
%A 孙奋勇
%J 中国生物工程杂志
%D 2006
%I 
%X Objective:To produce rhBMP-4 with bioactivity in E.coli. Methods: The full-length human BMP-4 gene was mutated by PCR without changes in amino acid sequence, then the synthesized gene was cloned into plasmid pET-3c, transducted into BL21(DE)plysS, and induced by adding IPTG to a final concentration of 1.0 mmol/L. The protein product was purified using ion-exchange chromatography method and then renaturated, bioactivity was checked by C2C12 differentiation in vitro and mouse ectopic bone formation in vivo. Results: A 438 bp gene fragment encoding mature peptide of hBMP-4 was cloned , the protein product was mostly in the form of inclusion body, after renaturation, the engineering protein shows better bioactivity. Conclusion:The mutant strategy can enhance the expression of bioactive rhBMP-4 in E.coli expression system.
%K rhBMP-4<br>定点突变
%K 包涵
%K 体活性
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=951380788B355DEA7D75520FA3B199C9&aid=FC43C3180F46FDA9&yid=37904DC365DD7266&vid=96C778EE049EE47D&iid=38B194292C032A66&sid=987EDA49D8A7A635&eid=014B591DF029732F&journal_id=1671-8135&journal_name=中国生物工程杂志&referenced_num=0&reference_num=14