Studies on enantioselectivities of avidin, avidin-biotin complex and streptavidin by affinity capillary electrophoresis

被引：1

作者：

Y. Tanaka

S. Terabe

机构：

[1] Nippon Boehringer Ingelheim Co. Ltd.,Department of Analytical Chemistry

[2] Himeji Institute of Technology,Department of Material Science, Faculty of Science

来源：

Chromatographia | 1999年 / 49卷

关键词：

Affinity capillary electrophoresis; Enantiomer separation; Egg white avidin and succinylated avidin; Streptavidin and avidin-biotin complex;

D O I：

暂无

中图分类号：

学科分类号：

摘要：

Various enantiomer separations were performed by affinity capillary electrophoresis with a partial filling technique (PFACE) using egg white avidin (AVI) and two avidin analogues: succinylated avidin (Suc-AVI) and streptavidin (STAV). Basic AVI was useful for enantiomer separation of acidic racemates, while the chemical modified acidic Suc-AVI was useful for that of basic racemates. Such a chemical modification of protein was effective in extending the applicability of the chiral selector in PFACE. STAV, which was a neutral nonglycosylated protein, was useful for both acidic and basic enantiomer separations. Although AVI and AVI analogues show similar biotin-binding activities, enantioselectivity was different among the proteins in this study. Additionally, we investigated whether the enantioselectivity was due to interaction of enantiomers with biotin-binding sites or not. Not only enantioselevtivity but also interaction with enantiomers was entirely lost by the formation of AVI-biotin complex.

引用

页码：489 / 495

页数：6

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