%0 Journal Article
%T Isolation, Purification and Renaturation of Recombinant-DNA-Derived Porcine Sonatotropin<br>基因工程猪生长激素的分离提纯及变复性技术的研究
%A LI Zhen
%A YU Rui-Song LIU Hui-Li WANG Ying ZHANG Ping ZHOU Zhi-Ai ZHANG De-Fu
%A <br>李震
%A 于瑞嵩
%A 张平
%A 王英
%A 刘惠莉
%J 生物工程学报
%D 2001
%I 
%X Large scale abstraction and isolation of bacterially synthesized, recombinant-DNA-derived, porcine growth hormone (r-pST) is described. The r-pGH is found in genetic engineering E.coli as the form of inclusion bodies. Pellet fraction which were mainly inclusion bodies, after cell breakage and centrifugation, were collected. Cell envelope components, such as protein, lipid, endotoxin and nucleic acids are selectively removed from the pellet fraction by an EDTA/lysozyme/deoxycholate extraction. Inclusion bodies were dissolved using 6mol/L guanidine/HCl and air oxidation is then carried out in the presence of the guanidine/HCl. The Guanidine/HCl protein mixture were diluted by renaturation solution. Guanidine/HCl were removed by dialysis and then correctly refolded, oxidized r-pGH were obtained. Injection experiment of hypophysectomized rats proved r-pST with high native bioactivity was obtained.
%K rPGH
%K isolation
%K renaturation<br>rPGH
%K 分离提纯
%K 变复性
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A66E90C274451689E69F6F0291467824&aid=116BC192968AA23B&yid=14E7EF987E4155E6&vid=BCA2697F357F2001&iid=B31275AF3241DB2D&sid=7D2B339649A57040&eid=703F3C1B6594BA64&journal_id=1000-3061&journal_name=生物工程学报&referenced_num=8&reference_num=6