SALT CONCENTRATION EFFECTS IN HIGH-PERFORMANCE HYDROPHOBIC-INTERACTION CHROMATOGRAPHY IN COMPARISON WITH NMR OF PROTEINS IN SOLUTION

被引：4

作者：

CORRADINI, D ^{[1
]}

CAPITANI, D ^{[1
]}

CELLAI, L ^{[1
]}

机构：

[1] CNR,IST STRUTTURIST CHIM,I-00016 MONTEROTONDO,ITALY

来源：

JOURNAL OF LIQUID CHROMATOGRAPHY | 1994年 / 17卷 / 20期

关键词：

D O I：

10.1080/10826079408013621

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The effects of salt concentration on the chromatographic behavior of cytochrome C, ribonuclease A, and alpha-chymotrypsinogen A in hydrophobic interaction chromatography (HIC) has been examined by isocratic elutions on a Bio-Gel TSK Phenyl 5 PW column. In some cases, conformational variations were manifest chromatographically by reproducible changes in peak shape and appearance of multiple peaks as a function of sodium sulfate concentration in the mobile phase. A parallel study by proton nuclear magnetic resonance (NMR) spectroscopy on the salt concentration dependence of the spectral property of these proteins is in agreement with the possible contribution of the mobile phase composition to the observed chromatographic behavior.

引用

页码：4335 / 4347

页数：13

共 31 条

[1] PREFERENTIAL INTERACTIONS OF PROTEINS WITH SALTS IN CONCENTRATED-SOLUTIONS [J].