The influence of mixed salts on the capacity of HIC adsorbers: A predictive correlation to the surface tension and the aggregation temperature
Author:
Affiliation:
1. Institute of Process Engineering in Life Sciences, Section IV: Biomolecular Separation Engineering; Karlsruhe Institute of Technology (KIT); Karlsruhe Germany
Funder
German Federal Ministry of Education and Research (BMBF)
Publisher
Wiley
Subject
Biotechnology
Reference21 articles.
1. Protein adsorption isotherm behavior in hydrophobic interaction chromatography;Chen;J Chromatogr A.,2007
2. Hydrophobic interaction chromatography of proteins III. Unfolding of proteins upon adsorption;Jungbauer;J Chromatogr A.,2005
3. Hydrophobic interaction chromatography of proteins II. Binding capacity, recovery and mass transfer properties;Hahn;J Chromatogr B.,2003
4. Hydrophobic interaction chromatography of homo-oligonucleotides on derivatized sepharose CL-6B. Using and relating two different models for describing the effect of salt and temperature on retention;Diogo;J Chromatogr A.,2003
5. Comparison of standard and new generation hydrophobic interaction chromatography resins in the monoclonal antibody purification process;Chen;J Chromatogr A.,2008
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1. Influence of mixed salts on retention behavior of model proteins in cation exchange chromatography;Journal of Chromatography A;2023-05
2. Protein-protein interactions and reduced excluded volume increase dynamic binding capacity of dual salt systems in hydrophobic interaction chromatography;Journal of Chromatography A;2021-07
3. Calorimetry for studying the adsorption of proteins in hydrophobic interaction chromatography;Preparative Biochemistry and Biotechnology;2019-01-02
4. Mathematical modeling of adsorption isotherms in mixed salt systems in hydrophobic interaction chromatography;Biotechnology Progress;2018-09
5. Influence of mixed electrolytes and pH on adsorption of bovine serum albumin in hydrophobic interaction chromatography;Journal of Chromatography A;2017-10
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