Adsorption of succinylated lysozyme on hydroxyapatite

被引：49

作者：

Barroug, A

Fastrez, J

Lemaitre, J

Rouxhet, P

机构：

[1] UNIV CATHOLIQUE LOUVAIN,FAC SCI,DEPT BIOL,B-1348 LOUVAIN,BELGIUM

[2] ECOLE POLYTECH FED LAUSANNE,LAB TECHNOL POUDRES,CH-1015 LAUSANNE,SWITZERLAND

[3] FAC SCI AGRON,UNITE CHIM INTERFACES,B-1348 LOUVAIN,BELGIUM

来源：

JOURNAL OF COLLOID AND INTERFACE SCIENCE | 1997年 / 189卷 / 01期

关键词：

hydroxyapatite; adsorption; lysozyme adsorption; succinylated lysozyme; zeta potential; hydrophobic interactions;

D O I：

10.1006/jcis.1997.4787

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Hen egg white lysozyme has been succinylated, the isoelectric point being shifted thereby from about 11 to 4.5-4.7. Its adsorption on a chromatography grade hydroxyapatite has been investigated at 20 degrees C and in the pH range from 5.9 to 7.4. Adsorption takes place despite an electrical repulsion between the surface and the adsorbate; consequently, it is favored by a decrease of pH and phosphate concentration and an increase of calcium concentration and ionic strength. While adsorption of native lysozyme is driven by electrostatic attraction to the surface, adsorption of succinylated lysozyme is controlled by hydrophobic interactions. This may be attributed to a different structure of modified lysozyme, compared to native lysozyme, or to a greater tendency to undergo conformational changes. (C) 1997 Academic Press.

引用

页码：37 / 42

页数：6

共 24 条

[1] THE BEHAVIOR OF SOME MODEL PROTEINS AT SOLID LIQUID INTERFACES .1. ADSORPTION FROM SINGLE PROTEIN SOLUTIONS [J].