Suitability of commercial hydrophobic interaction sorbents for temperature-controlled protein liquid chromatography under low salt conditions

► Temperature-dependent adsorption behavior of model proteins on HIC gels. ► Temperature as advantageous parameter regarding purification applications using HIC. ► Non-isothermal HIC resin regeneration. ► Temperature-mediated protein fractionation. ► Protein unfolding in dependence of ionic strength...

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Veröffentlicht in:	Journal of Chromatography A 2012-10, Vol.1260, p.88-96
Hauptverfasser:	Müller, Tobias K.H., Franzreb, Matthias
Format:	Artikel
Sprache:	eng
Schlagworte:	adsorbents Adsorption agarose ammonium sulfate Ammonium Sulfate - chemistry Animals bovine serum albumin Cattle Chromatography, Liquid - instrumentation Chromatography, Liquid - methods desorption Electrophoresis, Polyacrylamide Gel Hydrophobic and Hydrophilic Interactions hydrophobic bonding Hydrophobic interaction chromatography liquid chromatography lysozyme Partial protein unfolding processing stages Protein Binding Protein fractionation Protein Unfolding Resin regeneration resins Sepharose - chemistry Serum Albumin, Bovine - chemistry Serum Albumin, Bovine - metabolism sorption isotherms temperature Temperature effect Thermodynamics
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