A new thermodynamic model describes the effects of ligand density and type, salt concentration and protein species in hydrophobic interaction chromatography

Journal of Chromatography A

Volumn 1217, Issue 2, 2010, Pages 199-208

  Deitcher, R W ^a   Rome, J E ^a   Gildea, P A ^a   O'Connell, J P ^a   Fernandez, E J ^a  

^a University of Virginia   (United States)

Author keywords

Ligand density; Protein adsorption isotherm; Protein adsorption thermodynamics; Retention model

Indexed keywords

GLOBULAR PROTEINS; HYDROPHOBIC INTERACTION CHROMATOGRAPHY; HYDROPHOBIC INTERFACE; ISOCRATIC; LIGAND DENSITY; LOADING DATA; PROTEIN ADSORPTION; PROTEIN RETENTION; PROTEIN SPECIES; REPRODUCIBILITIES; RESPONSE BEHAVIOR; RETENTION MODELS; SALT CONCENTRATION; SOLVENT ACTIVITY; THERMODYNAMIC MODEL; WATER DISPLACEMENT;

ADSORPTION; ADSORPTION ISOTHERMS; CHROMATOGRAPHIC ANALYSIS; GEL PERMEATION CHROMATOGRAPHY; HYDROPHOBIC CHROMATOGRAPHY; HYDROPHOBICITY; LIGANDS; RESINS; THERMODYNAMIC PROPERTIES;

PROTEINS;

ALPHA LACTALBUMIN; CARBONATE DEHYDRATASE; GLOBULAR PROTEIN; LYSOZYME; OVALBUMIN; RESIN; SODIUM CHLORIDE;

ADSORPTION; ARTICLE; CHROMATOGRAPHY; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; DENSITY; HYDROPHOBICITY; ISOCRATIC ELUTION CHROMATOGRAPHY; ISOTHERMAL TITRATION CALORIMETRY; LIGAND BINDING; LOADING TEST; NONHUMAN; PRIORITY JOURNAL; REPRODUCIBILITY; SOLVENT EFFECT; THERMODYNAMICS;

ADSORPTION; ALGORITHMS; CHROMATOGRAPHY, LIQUID; HYDROPHOBICITY; LIGANDS; MODELS, CHEMICAL; PROTEINS; REPRODUCIBILITY OF RESULTS; SEPHAROSE; THERMODYNAMICS; WATER;

EID: 72449208847     PISSN: 00219673     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chroma.2009.07.068     Document Type: Article

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