Determination of cationic mobilities and pKa values of 22 amino acids by capillary zone electrophoresis
Language English Country Germany Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Amino Acids isolation & purification MeSH
- Electrophoresis, Capillary methods MeSH
- Cations MeSH
- Kinetics MeSH
- Hydrogen-Ion Concentration MeSH
- Computer Simulation MeSH
- Models, Theoretical MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Amino Acids MeSH
- Cations MeSH
The effective mobilities of the cationic forms of common amino acids--mostly proteinogenic--were determined by capillary zone electrophoresis in acidic background electrolytes at pH between 2.0 and 3.2. The underivatized amino acids were detected by the double contactless conductivity detector. Experimentally measured effective mobilities were fitted with the suitable regression functions in dependence on pH of the background electrolyte. The parameters of the given regression function corresponded to the values of the actual mobilities and the mixed dissociation constants (combining activities and concentrations) of the compound related to the actual ionic strength. McInnes approximation and Onsager theory were used to obtain thermodynamic dissociation constants (pK(a)) and limiting (absolute) ionic mobilities.
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