%0 Journal Article
%T Study on Optimization of Expression, Purification, Properties and Biological Function of Recombinant Human sBLyS<br>重组人sBLyS表达纯化条件的优化、理化特征及生物功能研究
%A YAN Xiao-Mei ZHANG Shuang-Quan ZHANG Da-Peng LIU Mei-Yan LIU Ping
%A <br>闫晓梅
%A 张双全
%A 张大鹏
%A 刘美艳
%A 刘平
%J 生物工程学报
%D 2002
%I 
%X The prokaryotic expression plasmid pET-30a(+)/sBLyS was constructed and transformed into E. coli BL21 (lambda DE3). The recombinant protein was found to be highly expressed by the plight of soluble part and inclusion body. For the sake of enhancing the proportion of the soluble part, inducement at 16 degrees C for 12 h was ascertained. The expressing product was then purified by Ni2+ affinity chromatography gel. PI of the recombinant human sBLyS(rhsBLyS) is about 7.1-7.3 and it assembles into a homotrimer. The effect of rhsBLyS on B lymphocytes by MTT method told us the B lymphocytes' proliferating capacity dose depended on concentration and also stimulating time of the rhsBLys. With rhsBLyS(2 micrograms/mL) stimulating 3 days, B lymphocytes can proliferate the most.
%K recombination human sBLyS
%K purification
%K homotrimer
%K cell proliferation<br>重组人sBLyS，
%K 纯化，
%K 同源三聚体，
%K 细胞增殖
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A66E90C274451689E69F6F0291467824&aid=E493CD305EF3C0FF&yid=C3ACC247184A22C1&vid=13553B2D12F347E8&iid=38B194292C032A66&sid=3C6F5C97A07587AE&eid=3224764AEAFCF8C2&journal_id=1000-3061&journal_name=生物工程学报&referenced_num=0&reference_num=13