%0 Journal Article
%T High Expression, Purification, Quality Control of rhEPO-Fc Fusion Protein<br>rhEPO-Fc融合蛋白的表达、纯化及质量研究
%A YANG Jian-jun
%A ZHANG Xin-jiong
%A ZHOU Jie
%A GONG Zheng
%A TAO Qun
%A YE Dan
%A WANG Shi-long
%A JU Dian-wen
%A <br>杨建军
%A 张昕泂
%A 周洁
%A 龚振
%A 陶群
%A 叶丹
%A 汪世龙
%A 鞠佃文
%J 中国生物工程杂志
%D 2007
%I 
%X To explore the technics for high expression, purification, quality control of recombinant human erythropoietin and IgG Fc fusion protein, rhEPO-Fc fusion protein expressed by CHO cells in serum-free medium was collected and purified with a three-step purification process-affinity chromatography, ion exchange chromatography and molecular sieve chromatography; and its quality was controlled by protein concentration, SDS-PAGE,Western-blot,HPLC,ELISA and IEF, et al. The research findings are that the expression output of rhEPO-Fc was highly reached 2g/L, the purify rate was over 45%, its purify was over 98%, its relative molecular weight is about 60kDa, t1/2 in vivo of rhEPO-Fc is over 38h, western blot analysis showed rhEPO-Fc has nature antigenicity. The expression output and purify rate of the produce technics is high, quality inspection methods are stability and reliable, which could be fit for in large-scale production of rhEPO-Fc.
%K Recombinant human erythropoietin Fc segment of immunoglo- bulin G Fusion protein The technics of fermentor and purify Quality control<br>重组人促红细胞生成素
%K 免疫球蛋白Fc段
%K 融合蛋白
%K 发酵纯化工艺
%K 质量研究
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=951380788B355DEA7D75520FA3B199C9&aid=9C23F5B78DD3E126&yid=A732AF04DDA03BB3&vid=DB817633AA4F79B9&iid=B31275AF3241DB2D&sid=B31275AF3241DB2D&eid=9CF7A0430CBB2DFD&journal_id=1671-8135&journal_name=中国生物工程杂志&referenced_num=0&reference_num=7