title: Study of the binding of antibiotics to human serum albumin by charge-transfer chromatography.
abstract: The interaction of 13 antibiotics with human serum albumin was studied by charge-transfer reversed-phase thin-layer chromatography in neutral, acidic, basic and ionic environments (NaCl and MgCl2) and the relative strength of interaction was calculated. The pH and the presence of mono- and divalent cations markedly influenced the strength of interaction. The capacity of antibiotics to interact with HSA also considerably depended on their chemical structure.
authors.affiliation: Central Research Institute for Chemistry, Hungarian Academy of Sciences, Budapest, Hungary.
authors.forename: T
authors.initials: T
authors.lastname: Cserháti
authors.forename: E
authors.initials: E
authors.lastname: Forgács
mesh_terms: D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000378:metabolism*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002855:Chromatography, Thin Layer; D006801:Humans; D006863:Hydrogen-Ion Concentration; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet
chemical_list: D000900:Anti-Bacterial Agents; D012709:Serum Albumin