ArticleScientific reports2021
Washing with alkaline solutions in protein A purification improves physicochemical properties of monoclonal antibodies.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 23 citations in OpenAlex.
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- Construction of an Immunosensor Based on the Affinity DNA Functional Ligands to the Fc Segment of IgG Antibody.Biosensors · 2025Article
- The administration of passive and active immunotherapy against Syntenin-1 decreased the tumoral growth and pulmonary metastasis in a murine model of triple-negative breast cancer.Scientific reports · 2025Article
- Cancer therapy via neoepitope-specific monoclonal antibody cocktails.Cancer immunology, immunotherapy : CII · 2025Article
- Determining buffer conditions for downstream processing of VLP-based recombinant hepatitis B surface antigen using multimodal resins in bind-elute and flow-through purification modes.Scientific reports · 2023Article
- Superantigen Recognition and Interactions: Functions, Mechanisms and Applications.Frontiers in immunology · 2021Review
Corrections and comments
- Erratum issued
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein A affinity chromatography has been widely used for both laboratory scale purification and commercial manufacturing of monoclonal antibodies and Fc-fusion proteins. Protein A purification is specific and efficient. However, there still remain several issues to be addressed, such as incomplete clearance of impurities including host cell proteins, DNA, aggregates, etc. In addition, the effects of wash buffers in protein A purification on the physicochemical characteristics of antibodies have yet to be fully understood. Here we found a new purification protocol for monoclonal antibodies that can improve physicochemical properties of monoclonal antibodies simply by inserting an additional wash step with a basic buffer after the capture step to the conventional protein A purification. The effects of the alkaline wash on monoclonal antibodies were investigated in terms of physicochemical characteristics, yields, and impurity clearance. The simple insertion of an alkaline wash step resulted in protection of antibodies from irreversible aggregation, reduction in free thiols and impurities, an improvement in colloidal and storage stability, and enhanced yields. This new procedure is widely applicable to protein A affinity chromatography of monoclonal antibodies.
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