%0 Journal Article
%T Expression of rhEPO-L-Fc Fusion Protein and Analysis of Its Bioactivity and Pharmacokinetics<br>rhEPO-L-Fc融合蛋白的表达、生物活性和初步药动学分析
%A Qiang Zhu
%A Zhihua Huang
%A Yuliang Huang
%A Yang Qin
%A <br>祝强
%A 黄智华
%A 黄予良
%A 覃扬
%J 生物工程学报
%D 2008
%I 
%X To prolong serum half-life of human Erythropoietin for better efficacy, a new form of recombinant human erythropoietin (rhEpo-L-Fc) was generated by fusion of a full length human erythropoietin gene and the Fc fragment of human IgG1 with flexible linker sequence. The fusion gene rhEPO-L-Fc was constructed by PCR, then inserted into expression vector pOptiVEC?-TOPO?, and expressed in Chinese Hamster Ovary cells deficient in the DHFR enzyme(CHO-dhfr-). The chimeric protein was purified by Protein A affinity chromatography, showed expected molecular weight and demonstrated a similar bioactivity compared to that of the native recombinant human erythropoietin (rhEPO) in an EPO-dependent cell-based assay. In vivo pharmacokinetic studies showed that the rhEPO-L-Fc had an elimination half-life of 27 h. In vivo efficacy studies showed that a single dose administration of rhEPO-L-Fc in rats increased the reticulocyte number in the peripheral blood significantly. These results demonstrated that the new engineered rhEPO-L-Fc may become alternative therapeutic approach to extend the half-time of rhEPO to treat anemia.
%K rhEPO-L-Fc fusion protein
%K half-life
%K CHO expression<br>rhEPO-L-Fc融合蛋白
%K 半衰期
%K CHO细胞表达
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A66E90C274451689E69F6F0291467824&aid=0C971D9E31F2C9B872E7F4F1FD616C5F&yid=67289AFF6305E306&vid=B91E8C6D6FE990DB&iid=708DD6B15D2464E8&sid=11C933E0BC2B8917&eid=ADEE850E40E2F1AA&journal_id=1000-3061&journal_name=生物工程学报&referenced_num=2&reference_num=13