The effectiveness of three multi-component binding models in describing the binary competitive equilibrium adsorption of two cytochrome b(5) mutants.
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.
Cano
Tony
T
Department of Chemical Engineering, University of Houston, 4800 Calhoun Ave., Houston, TX 77204-4004, USA.
Offringa
Natalie
N
Willson
Richard C
RC
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
D011994:Recombinant Proteins; D045303:Cytochromes b