Dynamic binding capacity (DBC) measurements of cation-exchange resins were performed with two human monoclonal antibodies. DBC showed a pH dependent maximum, which was shifted to lower pH values with increasing buffer concentrations and increasing salting-out effect of the buffer anion according to the Hofmeister series. As this downshift correlates well with zeta potential values, a measurement of the latter allows the determination of the pH value for maximum DBC under a given set of conditions. Thus, the use of zeta potential values can accelerate the purification process development and helps to understand the protein adsorption mechanism.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1016/j.chroma.2007.03.114 | DOI Listing |
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!