HYDROPHOBIC INTERACTION CHROMATOGRAPHY OF PROTEINS ON AN ALKYL-SUPEROSE COLUMN

被引：26

作者：

RIPPEL, G

SZEPESY, L

机构：

[1] TECH UNIV BUDAPEST, DEPT CHEM TECHNOL, BUDAFOKI 8, H-1521 BUDAPEST, HUNGARY

[2] TECH UNIV BUDAPEST, DEPT AGR CHEM TECHNOL, H-1521 BUDAPEST, HUNGARY

来源：

JOURNAL OF CHROMATOGRAPHY A | 1994年 / 664卷 / 01期

关键词：

D O I：

10.1016/0021-9673(94)80624-1

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The effects of ammonium sulphate, sodium acetate and sodium citrate on the retention of proteins were investigated under gradient conditions on an Alkyl-Superose column. It was found that the salts exert different effects on the retentions of hydrophobic and hydrophilic proteins. Retention data were evaluated according to the linear solvent strength theory of gradient elution. The calculated In k-salt molality relationships revealed specific and complex effects of the different salts on the retention behaviour of the proteins having different hydrophobicities.

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页码：27 / 32

页数：6

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