Clayton A. Brooks

TL;DR: A steric mass-action (SMA) ion-exchange equilibrium formalism is presented, which explicitly accounts for the steric hindrance of salt counterions upon protein binding in multicomponent equilibria, and the analytical solution of ideal isotachic displacement profiles with the SMA formalism enables rapid methods development and optimization of ion-Exchange displacement separations.

TL;DR: The results indicate that variable region interactions play a major role in determining elution pH for VH3 subfamily antibodies while using traditional protein A chromatographic materials, and experiments with a resin which employs a ligand consisting solely of B domain of Protein A indicate thatVariable region interactions can be mitigated, enabling the use of a single elutions pH for a range of antibodies.

TL;DR: In this paper, a wide range of antibodies from various subclasses and subfamilies are employed to evaluate the creation of generic separation processes using Protein A chromatography and the results indicate that variable region interactions play a major role in determining elution pH for VH3 subfamily antibodies while using traditional protein A chromatographic materials.

TL;DR: The effect of an alternate strategy employing two different flowrates during loading was explored as a means of increasing system productivity in Protein‐A chromatography and was found to result in significant improvements in process throughput.