INTERFACIAL THERMODYNAMICS OF PROTEIN ADSORPTION, ION COADSORPTION AND ION BINDING IN SOLUTION .2. MODEL INTERPRETATION OF ION-EXCHANGE IN LYSOZYME CHROMATOGRAPHY

被引:12
作者
FRAAIJE, JGEM [1 ]
NORDE, W [1 ]
LYKLEMA, J [1 ]
机构
[1] AGR UNIV WAGENINGEN,DEPT PHYS & COLLOID CHEM,6703 HB WAGENINGEN,NETHERLANDS
关键词
PROTEINS; THERMODYNAMICS; ADSORPTION; ION COADSORPTION; ION EXCHANGE CHROMATOGRAPHY; LYSOZYME;
D O I
10.1016/0301-4622(91)80029-Q
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
In this paper we present a model for the ion exchange effects in protein adsorption. The model is applied to chromatography of lysozyme on strong cation exchanger 'mono S'. The experimental and general thermodynamic aspects have been discussed in Part 1, the preceding paper. The main modelling assumptions are (i) the charge regulation is confined to the small layer of contact between adsorbed protein and exchanger surface, (ii) the contact layer as a whole is electroneutral and (iii) the number of protein acid/base groups and exchanger surface acid groups which participate in the ion exchange is proportional to the area of the contact layer. The model is fitted to the experimental data by adjustment of only two or three parameters. The experimental co-adsorption numbers are very well reproduced. A few conspicuous features emerge: (i) the number of protein acid/base groups and exchanger surface acid groups in the contact layer varies with the medium conditions, such that the number is higher when the interaction between protein and exchanger surface is stronger. (ii) There is indirect evidence for structural alterations in the upper layers of the exchanger surface: the adsorbed protein is probably partly 'buried' in the surface.
引用
收藏
页码:317 / 327
页数:11
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