title: The effectiveness of three multi-component binding models in describing the binary competitive equilibrium adsorption of two cytochrome b(5) mutants.
abstract: Competitive adsorption isotherms for two conservative surface charge-neutralizing mutants of cytochrome b(5), E11Q and E44Q, previously measured with competitor concentration held constant over the range of the isotherm, were used to test three widely-used multi-component isotherm models. The extended Langmuir-Freundlich, Langmuir and Jovanovic-Freundlich models each adequately described the weaker infinite dilution adsorption of the E44Q protein in the presence of the strong binding E11Q. The extended Langmuir-Freundlich model generally gave the lowest errors at higher concentrations, and the Jovanovic-Freundlich model gave the best fits when using empirically optimized maximal loading values based on multi-component as well as pure-component isotherm data.
authors.affiliation: Department of Chemical Engineering, University of Houston, 4800 Calhoun Ave., Houston, TX 77204-4004, USA.
authors.forename: Tony
authors.initials: T
authors.lastname: Cano
authors.forename: Natalie
authors.initials: N
authors.lastname: Offringa
authors.forename: Richard C
authors.initials: RC
authors.lastname: Willson
mesh_terms: D000327:Adsorption; D001667:Binding, Competitive; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D045303:Cytochromes b / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification; D007474:Ion Exchange; D008954:Models, Biological; D008956:Models, Chemical; D009154:Mutation; D011485:Protein Binding; D011994:Recombinant Proteins; D013499:Surface Properties; D013816:Thermodynamics
chemical_list: D011994:Recombinant Proteins; D045303:Cytochromes b