title: Chromatographic and fluorometric study of interactions between thiophilic and hydrophobic ligands and tryptophan peptide homologues.
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".
authors.affiliation: Institute of Molecular and Cell Biology, 61 Biopolis Drive, Proteos, Singapore 138673, Singapore.
authors.forename: Bo
authors.initials: B
authors.lastname: Xue
authors.forename: Bo
authors.initials: B
authors.lastname: Ersson
authors.forename: Jerker
authors.initials: J
authors.lastname: Porath
authors.forename: Karin
authors.initials: K
authors.lastname: Caldwell
mesh_terms: D002853:Chromatography, Liquid / Q000379:methods*; D006863:Hydrogen-Ion Concentration; D008024:Ligands; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D012492:Salts; D013050:Spectrometry, Fluorescence / Q000379:methods*; D013056:Spectrophotometry, Ultraviolet; D013696:Temperature; D014364:Tryptophan / Q000378:metabolism*
chemical_list: D008024:Ligands; D010455:Peptides; D012492:Salts; D014364:Tryptophan