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用于毛细管电泳中碱性蛋白质分离的有效离子对作用。

Effective ion-pairing for the separation of basic proteins in capillary electrophoresis.

作者信息

Okafo G N, Vinther A, Kornfelt T, Camilleri P

机构信息

SmithKline Beecham Pharmaceuticals, Frythe, Welwyn, Herts, UK.

出版信息

Electrophoresis. 1995 Oct;16(10):1917-21. doi: 10.1002/elps.11501601316.

DOI:10.1002/elps.11501601316
PMID:8586065
Abstract

The addition of the sodium salt of phytic acid to the separation buffer (pH's 6.0-9.5) has allowed the analysis of a number of basic proteins (pI's > 9) by capillary electrophoresis. The method of analysis is simple and leads to considerable improvement in peak shape. Some very basic proteins, totally adsorbed onto the capillary fused silica surfaces in the presence of buffer only, can be analysed as sharp signals when this polyanionic species is included in the running electrolyte. These improvements in analysis are thought to arise as a result of the suppression of coulombic interactions between these positively charged proteins (ion-paired to phytic acid) and the negatively charged silanol groups on the inner wall of the capillary.

摘要

在分离缓冲液(pH值为6.0 - 9.5)中添加植酸钠,使得通过毛细管电泳能够分析多种碱性蛋白质(等电点> 9)。分析方法简单,并且能显著改善峰形。一些非常碱性的蛋白质,在仅存在缓冲液时会完全吸附在毛细管熔融石英表面,而当这种聚阴离子物质包含在运行电解质中时,可以作为尖锐信号进行分析。分析中的这些改进被认为是由于抑制了这些带正电荷的蛋白质(与植酸形成离子对)与毛细管内壁带负电荷的硅醇基团之间的库仑相互作用。

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