Autor: |
Matyska, M. T., Pesek, J. J., Chen, J. I-Chen, Boysen, R. I., Hearn, M. T. W. |
Zdroj: |
Chromatographia; Apr2005, Vol. 61 Issue 7/8, p351-357, 7p |
Abstrakt: |
This study investigates the impact of peptide primary structure and the characteristics of two different types of immobilised hydrophobic ligands on the open tubular electro-chromatographic migration behaviour of a family of related synthetic peptide analogues. The results further document the important role that mixed mode electrophoretic/chromatographic processes play in determining peptide selectivity in OTCEC systems. Procedures to fine-tune selectivity of closely related peptides in these systems have been established with buffer electrolytes of different composition in terms of the organic solvent content and different pH conditions. [ABSTRACT FROM AUTHOR] |
Databáze: |
Complementary Index |
Externí odkaz: |
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