THE EFFECT OF SURFACE HYDROPHOBICITY AND PROTEIN-CONCENTRATION ON BUFFER CRYSTALLIZATION AND ELISA ABSORBENCY

被引：5

作者：

GEDDES, NJ

FURLONG, DN

ZIENTEK, P

THAN, KA

EDGAR, JA

机构：

[1] CSIRO,DIV CHEM & POLYMERS,CLAYTON,VIC 3168,AUSTRALIA

[2] CSIRO,DIV ANIM SCI,PARKVILLE,VIC 3052,AUSTRALIA

来源：

JOURNAL OF COLLOID AND INTERFACE SCIENCE | 1993年 / 157卷 / 02期

关键词：

D O I：

10.1006/jcis.1993.1212

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：

The crystallization of sodium carbonate buffer from a protein/buffer solution was found to be independent of the surface hydrophobicity when an absorbed protein layer was present. By contrast, the form of the carbonate crystallites was dependent on the protein concentration in solution, ELISA tests on the absorbed protein layer showed that the IgG component of the protein film was more enzymatically active on hydrophilic surfaces. © 1993 Academic Press Limited.

引用

页码：491 / 497

页数：7

共 13 条

[1] USE OF MICROWELL PLATES CARRYING HYDRAZIDE GROUPS TO ENHANCE ANTIBODY IMMOBILIZATION IN ENZYME IMMUNOASSAYS [J].