After model calibration from chromatograms of bind-and-elute experiments, results were validated with batch isotherms and prediction of further gradient elution chromatograms. The model's capability of describing column chromatography experiments is demonstrated with glucose oxidase, bovine serum albumin (BSA), and lysozyme on Capto™ Phenyl (high sub) as model system.
9 Therefore, it was expected that yeast expressed P2. Experimental results are presented for two different monoclonal antibodies and for lysozyme on Capto Phenyl (High Sub) resin. Capto Phenyl hign subACapto ButylBpH1-4401TOC. coli expressed material, after the removal of HCP by anion exchange. 3.7 Hydrophobic interaction chromatography HIC is used as a bind-elute step in the published protocol based on E. Capto Phenyl (High sub) and Capto Butyl are hydrophobic interaction chromatography (HIC) resins used in the capture and intermediate stages. size find -GE17545908 MSDS, related peer-reviewed papers, technical documents, similar products & more at Sigma-Aldrich. In this work, a new mechanistic isotherm model for HIC is derived by consideration of an equilibrium between well-ordered water molecules and bulk-like ordered water molecules on the hydrophobic surfaces of protein and ligand. These were: HIC Capto Phenyl (High Sub) multimodal Nuvia C Prime cation exchange Capto S ImpAct. HiTrap® Capto Butyl pkg of 5 × 1 mL, Cytiva, 17-5459-08, 75 m avg. As a combination of these two techniques is often encountered in biopharmaceutical purification steps, accurate modeling of protein adsorption in HIC is a core issue for applying holistic model-based process development, especially in the light of the Quality by Design (QbD) approach. Modeling and simulation of hydrophobic interaction chromatography (HIC) in the column mode has been seldom reported. Mechanistic models are successfully used for protein purification process development as shown for ion-exchange column chromatography (IEX).
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