A new thermodynamic model describes the effects of ligand density and type, salt concentration and protein species in hydrophobic interaction chromatography.
A new thermodynamic model is derived that describes both loading and pulse-response behavior of proteins in hydrophobic interaction chromatography (HIC). The model describes adsorption in terms of protein and solvent activities, and water displacement from hydrophobic interfaces, and distinguishes contributions from ligand density, ligand type and protein species. Experimental isocratic response and loading data for a set of globular proteins on Sepharose resins of various ligand types and densities are described by the model with a limited number of parameters. The model is explicit in ligand density and may provide insight into the sensitivity of protein retention to ligand density in HIC as well as the limited reproducibility of HIC data.
Deitcher
R W
RW
Department of Chemical Engineering, University of Virginia, Charlottesville, VA 22904-4741, USA.
Rome
J E
JE
Gildea
P A
PA
O'Connell
J P
JP
Fernandez
E J
EJ
D000327:Adsorption; D000465:Algorithms; D002853:Chromatography, Liquid / Q000379:methods*; D057927:Hydrophobic and Hydrophilic Interactions; D008024:Ligands; D008956:Models, Chemical; D011506:Proteins / Q000737:chemistry*; D015203:Reproducibility of Results; D012685:Sepharose / Q000737:chemistry; D013816:Thermodynamics; D014867:Water / Q000737:chemistry
D008024:Ligands; D011506:Proteins; D014867:Water; D012685:Sepharose
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