| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1211638 | Journal of Chromatography A | 2006 | 6 Pages |
Abstract
The interactions of tryptophan and its peptide homologues with thiophilic ligands were studied in terms of their chromatographic retention and steady-state fluorescence under various conditions, and compared with non-polar structures typically regarded as pure hydrophobic ligands. The experimental results show that both non-polar and polar interactions are involved in what has been termed “thiophilic adsorption chromatography”.
Related Topics
Physical Sciences and Engineering
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Authors
Bo Xue, Bo Ersson, Jerker Porath, Karin Caldwell,