PEG蛋白质分离纯化的新方法  

New Method for Separation and Purification of PEG-protein

作　　者：唐微[1] 常远[1] 邱雪贞[1] 郑仲承[1] 刘新垣[1] 

机构地区：[1]中国科学院上海生物化学研究所

出　　处：《生物化学杂志》1996年第1期73-77,共5页

摘　　要：ＰＥＧ化蛋白质的分离纯化比较困难，本工作发现ＰＥＧ化蛋白质仍能被硫酸铵盐析，据此可以简单地将ＩＬ－２及ＰＥＧ化ＩＬ－２沉淀出来，而将有毒的活化ＰＥＧ等副产物留在溶液中。此方法效果理想而又十分简便。文献中未见报道。此外，实验还发现，在ＰＥＧ－ＩＬ－２与ＩＬ－２的混和液中加入一定量的ＰＥＧ后，二者之间溶解度差别增大，当用ＳｅｐｈａｃｒｙⅠＳ－２００柱分离时，先用含１０％ＰＥＧ，０．２５ｍｏｌ／ＬＮａＣｌ的缓冲液平衡洗脱ＰＥＧ－ＩＬ－２，再降低盐浓度洗下ＩＬ－２，即可使二者完全分开。过去要将ＩＬ－２与ＰＥＧ－ＩＬ－２分离开非常困难，本工作解决了这个问题，这点亦未见文献报道。it is difficult to separate and purify PEG-protein. But now,it have been found that the PEG-protein may be salted-out by (NH_4)_2 SO_4) and the by-products stay still in the solution. It is a simple and speedy method reported about the separation. In addition,it was also found that,by adding some PEG to the mixture solution of PEG-IL-2 and IL-2,the difference between them can be increased. Then the mixture solution was applied on sephacry I S-200 column. The PEGIL-2 was eluted out with a buffer containing 10% PEG, 0. 25 mol/L NaCl at first,and followed by IL-2 when the PEG and salt had been removed So both were isolated completely,which was considered to be very difficult indicated in the literature. Also this method has never been reported.

关 键 词：蛋白 PEG蛋白 分离 提纯 

分 类 号：Q513.03[生物学—生物化学]