Background::
Protein A affinity chromatography is often employed as the most crucial purification step for monoclonal
antibodies to achieve high yield with purity and throughput requirements.
Introduction::
Protein A also known as Staphylococcal protein A (SPA) is found at cell wall of the bacteria staphylococcus
aureus. It is one of the first discovered immunoglobulin binding molecules and has been extensively studied during the past
decades. The efficiency of Protein A affinity chromatography to purify a recombinant monoclonal antibody in a cell culture
sample was evaluated, which removes 99.0 % of feed stream impurities.
Materials and Method::
We have systematically evaluated the purification performance by using a battery of analytical
methods SDS-PAGE (non-reduced and reduced sample), Cat ion Exchange Chromatography (CEX), Size-exclusion chromatography
(SEC), and Reversed phased-Reduced Chromatography for a CHO-derived monoclonal antibody.
Results and Discussion::
The analytical test was used to determine the impurity parameter, Host Cell Contaminating Proteins
(HCP), and was evaluated 0.015ng/ml after the purification step; initially it was found 24.431ng/ml.
Conclusion::
The tests showed that there was a distinct decrease in the level of different impurities after the chromatography
step. It can be concluded that Protein A chromatography is an efficient capture and polishing step in the purification of
monoclonal antibodies.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.