%0 Journal Article
%T Preliminary Study on the Purification of IL-2<br>纯化基因重组白细胞介素-2的初步研究
%A YAN Ying
%A HAO Qian
%A FAN Guo-liang
%A ZHAO Qiu-wen
%A LIU Ying-wu
%A WANG Jian-lin
%A WAN Dong-lin
%A <br>阎颖
%A 郝茜
%A 范国梁
%A 赵秋雯
%A 刘迎五
%A 王建林
%A 万冬林
%J 色谱
%D 2000
%I 
%X Interleukin-2 (IL-2) which is produced by T-lymphocytes is a protein molecule with the molecular weight of 15,420-Daltons. It has good functions in curing a lot of diseases such as cancer and AIDS even with a small quantity. A new method for purification of IL-2 by preparative high performance liquid chromatography is described. It was the first time to use hydroxyapatite as the packing to separate IL-2. IL-2 has one disulphide bridge (between 58th Cys and 105th Cys) and one free cysteine. In order to prevent aggregation and formation of wrong disulphide bond, 50 mumol/L Cu2+ and 1.5 mol/L guanidine hydrochloride was used for autoxidation and denaturing. Then we used mainly two chromatographic steps: First, Sephadex G-25 Gel permeation chromatography was used to separate guanidine hydrochloride and small molecules. Second, large scale preparative HPLC was used to separate impure protein from IL-2. Gradient elution was performed with phosphate buffer (pH 6.8). Its purity was examined by SDS-PAGE. Its activity reached 1 x 10(6) U/mg by CTLL-2 cell MTT method. The results showed that it is a suitable method for the large-scale purification of IL-2.
%K preparative high performance liquid chromatography
%K interleukin
%K 2
%K hydroxyapatite<br>基因重组白细胞介素－2
%K 分离提纯
%K HAP
%K HPLC
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=6E709DC38FA1D09A4B578DD0906875B5B44D4D294832BB8E&cid=6579068328FE643F&jid=4D81E042D77AFEC6881D14759692069C&aid=9BA2AC08419A7FD800453B66A2FCFE72&yid=9806D0D4EAA9BED3&vid=13553B2D12F347E8&iid=E158A972A605785F&sid=86C0C9A759FDA8CA&eid=170CE8B011EA4FD9&journal_id=1000-8713&journal_name=色谱&referenced_num=1&reference_num=9