title: Chlorpheniramine binding to human serum albumin by fluorescence quenching measurements.
abstract: The binding of chlorpheniramine to human serum albumin has been studied by fluorescence quenching, as a function of temperature; the experimental data could only be fitted to the Stern-Volmer modified equation. A statistical analysis of the results was performed in order to determine the significance of the constants calculated by this equation, as well as their thermodynamic parameters. The chlorpheniramine binding to human serum albumin accounts for almost half of the binding of this antihistaminic agent to human plasma proteins.
authors.affiliation: Departamento de Química Física Farmaceútica, Facultad de Farmacia, Universidad Complutense, Madrid, Spain.
authors.forename: J
authors.initials: J
authors.lastname: Gonzalez-Jimenez
authors.forename: G
authors.initials: G
authors.lastname: Frutos
authors.forename: I
authors.initials: I
authors.lastname: Cayre
authors.forename: M
authors.initials: M
authors.lastname: Cortijo
mesh_terms: D002744:Chlorpheniramine / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013816:Thermodynamics
chemical_list: D012709:Serum Albumin; D002744:Chlorpheniramine