In order to use micellar electrokinetic chromatography to determine the proteolytic activity of different proteinases simultaneously present in physiological fluids, the technique must be able to separate mixtures of substrates with closely related structures. In an attempt to determine the best ele
Separation of various positional isomers of aromatic anions by nonionic micellar electrokinetic chromatography coupled with ion association distribution
โ Scribed by Toshio Takayanagi; Kana Fushimi; Shoji Motomizu
- Publisher
- John Wiley and Sons
- Year
- 2000
- Tongue
- English
- Weight
- 113 KB
- Volume
- 12
- Category
- Article
- ISSN
- 1040-7685
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โฆ Synopsis
Separation of positional isomers of aromatic anions was studied by micellar electrokinetic chromatography using nonionic surfactants andror an ion association reagent. The isomers were well resolved by adding nonionic surfactant in the migrating solution, which indicates that binding of the anions to a nonionic surfactant micelle is different among the isomers. The apparent electrophoretic mobility of the anions decreased with increasing concentrations of the surfactants in the migrating solution, and the binding phenomena are analyzed from the electrophoretic mobility change. Addition of an ion association reagent in the migrating solution also changed the resolutions. Some binding constants of the ion associates are also determined through the mobility change.
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