%0 Journal Article
%T CLONING, EXPRESSION AND PURIFICATION OF THE CHAPERONIN GROESL IN ESCHER1CHIA COLI<br>分子伴侣GroESL在大肠杆菌中的克隆、表达及分离纯化
%A Zhou Ying Yin Changchuan Zhang Qing Song Daxin Chen Yongqing
%A <br>周颖
%A 殷长传
%A 张青
%A 宋大新
%A 陈永青
%J 微生物学报
%D 1997
%I 
%X The DNA fragment encoding the molecular chaperion GroESL was subcloned into high-expression vector pKC220, and the GroESL were high expressed in the E. coli strain harboring the recombinant plasmid by high temperature induction. The amount of the expressed GroEL and GroES protein were about 40% and 15% of the total cellular proteins, respectively. These two subunits were both purified from E. coli by (NH4)2SO4 salt out DEAE-52 chromography and Sephadex G-50 chromo-graphy.
%K Chaperonin
%K GroESL
%K High expression
%K Purification<br>分子伴侣
%K GroESL
%K 高效表达
%K 分离纯化
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A3C6BA55AB623B90FA9104CFFC826F3C&aid=72CD0394B7CA24DE41CFC22EB352CD30&yid=5370399DC954B911&vid=42425781F0B1C26E&iid=94C357A881DFC066&sid=A04F01817ECB9A48&eid=375BEEEA164CFE59&journal_id=0001-6209&journal_name=微生物学报&referenced_num=0&reference_num=0