Electrostatic model for protein adsorption in ion-exchange chromatography and application to monoclonal antibodies, lysozyme and chymotrypsinogen A

2010 ◽  
Vol 1217 (35) ◽  
pp. 5610-5621 ◽  
Author(s):  
Bertrand Guélat ◽  
Guido Ströhlein ◽  
Marco Lattuada ◽  
Massimo Morbidelli
Keyword(s):  
Monoclonal Antibodies ◽  
Ion Exchange ◽  
Protein Adsorption ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Electrostatic Model

scholarly journals Ion exchange chromatography of monoclonal antibodies: Effect of resin ligand density on dynamic binding capacity

2009 ◽  
Vol 1216 (20) ◽  
pp. 4366-4371 ◽  
Author(s):  
Ann Marie Hardin ◽  
Chithkala Harinarayan ◽  
Gunnar Malmquist ◽  
Andreas Axén ◽  
Robert van Reis
Keyword(s):  
Monoclonal Antibodies ◽  
Ion Exchange ◽  
Binding Capacity ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Dynamic Binding ◽  
Ligand Density ◽  
Dynamic Binding Capacity

Capillary ion-exchange chromatography with nanogram sensitivity for the analysis of monoclonal antibodies

2015 ◽  
Vol 1424 ◽  
pp. 77-85 ◽  
Author(s):  
Jennifer C. Rea ◽  
Benny S. Freistadt ◽  
Daniel McDonald ◽  
Dell Farnan ◽  
Yajun Jennifer Wang
Keyword(s):  
Monoclonal Antibodies ◽  
Ion Exchange ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography

scholarly journals Isothermal Titration Calorimetry as a Method for Analyzing Protein Adsorption in Ion Exchange Chromatography

2021 ◽  
Vol 333 ◽  
pp. 15001
Author(s):  
Joao Simoes-Cardoso ◽  
Nanako Hoshino ◽  
Noriko Yoshimoto ◽  
Shuichi Yamamoto
Keyword(s):  
Ion Exchange ◽  
Protein Adsorption ◽  
Isothermal Titration Calorimetry ◽  
Protein Interactions ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Titration Calorimetry ◽  
Valuable Insight ◽  
Adsorption Enthalpy ◽  
Binding Behavior

Ion exchange chromatography is a widely used method for purification of all types of biomolecules in current biotechnological downstream processes. Knowledge on the binding behavior of proteins provides valuable insight for understanding the molecular mechanisms of protein interactions in a biological context. However, thermodynamic parameters such as enthalpy and entropy changes that characterize protein adsorption are still unknown. Isothermal titration calorimetry applications in biosciences has gained its merit to study binding of soluble molecules, protein inhibition, conformational changes, reaction kinetics, and protein adsorption. However, in the case of protein adsorption, a lot of complications arise since the usual models used to study protein interactions in solution are no longer valid. This work explains a detailed methodology for the obtention of adsorption enthalpy, entropy and Gibbs energy of protein adsorption, by using ITC together with equilibrium adsorption isotherms.

Sign in / Sign up

Export Citation Format

Share Document