Adsorption of human carbonic anhydrase II onto silicon oxides surfaces: The effects of truncation in the N-terminal region

被引：0
|
作者：
Billsten, P [1 ]
Wahlgren, M [1 ]
Elwing, H [1 ]
机构：
[1] Linkoping Univ, JFM Lab Appl Phys, S-58183 Linkoping, Sweden
来源：
COLLOID SCIENCE OF LIPIDS: NEW PARADIGMS FOR SELF-ASSEMBLY IN SCIENCE AND TECHNOLOGY | 1998年 / 108卷
关键词：
protein adsorption; ellipsometry; carbonic anhydrase; mutant proteins; solid surfaces;
D O I：
暂无
中图分类号：
R914 [药物化学];
学科分类号：
100701 ;
摘要：
The adsorption of human carbonic anhydrase II pseudo-wild type (HCAII(pwt)) and an N-terminally truncated version thereof onto silica surfaces were studied. The amount adsorbed and the adsorption kinetics were measured using in situ ellipsometry. A substantial difference was seen between the two proteins. The adsorbed amount of the truncated version (2.53 mg/m(2)) indicates an end-on orientation, while the HCAII(pwt) seems to adsorb side-on (1.84 mg/m(2)). It is suggested that the orientation effects arise from the truncation. The truncation is known to unfold the two most N-terminal helical segments, which could inhibit adsorption with the N-terminal region facing the surface, due to steric repulsion.
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页码：161 / 165
页数：5
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