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Volumn 1157, Issue 1-2, 2007, Pages 197-206
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Generalizing a two-conformation model for describing salt and temperature effects on protein retention and stability in hydrophobic interaction chromatography
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Author keywords
Lactoglobulin; Gradient elution; Hydrophobic interaction chromatography; Isocratic elution; Protein adsorption
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Indexed keywords
ADSORPTION;
CHEMICAL STABILITY;
CHROMATOGRAPHIC ANALYSIS;
CONFORMATIONS;
SALTS;
THERMODYNAMIC PROPERTIES;
GRADIENT ELUTION;
HYDROPHOBIC INTERACTION CHROMATOGRAPHY (HIC);
ISOCRATIC ELUTION;
PROTEIN ADSORPTION;
RETENTION STRENGTH;
PROTEINS;
BENZENE DERIVATIVE;
BETA LACTOGLOBULIN;
PROTEIN;
SEPHAROSE;
SODIUM CHLORIDE;
ADSORPTION KINETICS;
ARTICLE;
BIOTECHNOLOGICAL PROCEDURES;
CALCULATION;
CHEMICAL MODEL;
CHROMATOGRAPHY;
CONCENTRATION (PARAMETERS);
ELUTION;
PREDICTION;
PRIORITY JOURNAL;
PROTEIN CONFORMATION;
PROTEIN FOLDING;
PROTEIN PROCESSING;
PROTEIN STABILITY;
TEMPERATURE;
THERMODYNAMICS;
CHROMATOGRAPHY, LIQUID;
MODELS, THEORETICAL;
PROTEIN CONFORMATION;
PROTEINS;
SALTS;
TEMPERATURE;
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EID: 34250767811
PISSN: 00219673
EISSN: None
Source Type: Journal
DOI: 10.1016/j.chroma.2007.05.009 Document Type: Article |
Times cited : (33)
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References (43)
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