Related Experiment Video
Updated: Jul 2, 2026

MultiBac System-Based Purification and Biophysical Characterization of Human Myosin-7a
Published on: August 23, 2024
Robustness of virus removal by protein A chromatography is independent of media lifetime
Scott Lute1, Lenore Norling, Michael Hanson
1Office of Biotechnology Products, Center for Drug Evaluation and Research, Food and Drug Administration, 10903 New Hampshire Avenue, Silver Spring, MD 20993, USA.
Abstract:
The robustness of virus clearance with respect to protein A media reuse was demonstrated using media with four matrix chemistries: Protein A immobilized ProSep A, Poros A50, Protein A ceramic Hyper DF and MabSelect SuRe, an alkali resistant protein A ligand. Endogenous retrovirus clearance, step yield, impurity clearance and other performance parameters were evaluated periodically in media cycled up to 300 times. Media lifetime was generally limited by either declining step yield or media fouling. However, clearance of endogenous retrovirus remained in an acceptable range, either increasing or remaining constant. Multiply cycled media were tested for clearance of three viruses (SV40, X-MuLV, and MMV); clearance was comparable to naïve media. Overall, virus clearance by protein A chromatography appears to be extremely robust with respect to media age.
More Related Videos
07:50Detection and Removal of Nuclease Contamination During Purification of Recombinant Prototype Foamy Virus Integrase
Published on: December 8, 2017
09:12Isolation of Adeno-Associated Viral Vectors Through a Single-Step and Semi-Automated Heparin Affinity Chromatography Protocol
Published on: April 5, 2024