Simultaneous removal of leached protein-A and aggregates from monoclonal antibody using hydrophobic interaction membrane chromatography
Journal of Membrane Science, ISSN: 0376-7388, Vol: 390, Page: 263-269
2012
- 20Citations
- 45Captures
Metric Options: Counts1 Year3 YearSelecting the 1-year or 3-year option will change the metrics count to percentiles, illustrating how an article or review compares to other articles or reviews within the selected time period in the same journal. Selecting the 1-year option compares the metrics against other articles/reviews that were also published in the same calendar year. Selecting the 3-year option compares the metrics against other articles/reviews that were also published in the same calendar year plus the two years prior.
Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Article Description
Protein-A affinity chromatography is the standard capture technique used for purification of monoclonal antibodies (mAbs). A major problem with this technique is its inability to remove monoclonal antibody aggregates from the monomeric form of the antibody. Moreover, the elution of mAbs from a protein-A column is carried out using acidic conditions which in turn could accelerate the formation of antibody aggregates and causes leaching of protein-A from its supporting media. These impurities have to be removed using appropriate separation methods before the mAb can be used for therapeutic applications. There is currently a limited repertoire of polishing techniques which simultaneously remove both mAb aggregates and protein-A. In this paper, we describe a polishing method based on hydrophobic interaction membrane chromatography for simultaneously removing these impurities. The flow-through mode was used whereby monomeric mAb flowed through a membrane stack while impurities were retained by reversible adsorption. These impurities were subsequently eluted by lowering the salt concentration and the membrane stack was thus regenerated. The operating conditions for this method were systematically optimized using pure mAb, aggregates, protein-A, and mAb/protein-A complexes. The mechanisms by which aggregates and leached protein-A were simultaneously removed are hypothesized.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0376738811008763; http://dx.doi.org/10.1016/j.memsci.2011.11.049; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84855273778&origin=inward; https://linkinghub.elsevier.com/retrieve/pii/S0376738811008763; https://dx.doi.org/10.1016/j.memsci.2011.11.049
Elsevier BV
Provide Feedback
Have ideas for a new metric? Would you like to see something else here?Let us know