PROTEIN SEPARATION AND PURIFICATION IN NEAT DIMETHYL-SULFOXIDE

被引：30

作者：

CHANG, N ^{[1
]}

HEN, SJ ^{[1
]}

KLIBANOV, AM ^{[1
]}

机构：

[1] MIT,DEPT CHEM,CAMBRIDGE,MA 02139

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 176卷 / 03期

基金：

美国国家科学基金会;

关键词：

D O I：

10.1016/0006-291X(91)90451-C

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Pure DMSO (instead of water) is used as the reaction medium for protein separations. It is shown that common extracellular proteins (i) have high solubility in DMSO (1-50 mg/ml), (ii) do not irreversibly inactivate in this solvent, and (iii) can adsorb onto carboxymethyl cellulose in DMSO and be subsequently fully desorbed in this solvent by inorganic salts. Ion-exchange chromatography on this resin in DMSO has been used to purify bovine pancreatic trypsin and to separate it from hen egg-white lysozyme in their mixture. Another approach to protein separation in DMSO, fractional precipitation with ethyl acetate (which does not dissolve proteins), has been verified with a mixture of bovine pancreatic chymotrypsinogen and chicken egg ovalbumin. © 1991.

引用

页码：1462 / 1468

页数：7

共 23 条

[1] METAL-AFFINITY SEPARATIONS - A NEW DIMENSION IN PROTEIN PROCESSING [J].