Secretory leukocyte protease inhibitor (SLPI) might contaminate murine monoclonal antibodies after purification on protein G
Autor: | Joerg Fettke, Christine Lenz, Jörg A. Schenk, Emely Kusch, Nenad Gajovic-Eichelmann, Eva Ehrentreich-Förster, Frank Sellrie, Katharina Albers, Frank Mallwitz |
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Přispěvatelé: | Publica |
Jazyk: | angličtina |
Rok vydání: | 2012 |
Předmět: |
medicine.drug_class
Bioengineering Monoclonal antibody Applied Microbiology and Biotechnology Chromatography Affinity Mice Bacterial Proteins Affinity chromatography Protein A/G medicine Animals Secretory Leukocyte Peptidase Inhibitor Staphylococcal Protein A Progesterone Institut für Biochemie und Biologie biology Antibodies Monoclonal General Medicine Molecular biology Protease inhibitor (biology) Antibodies Anti-Idiotypic Milk Biochemistry biology.protein Protein G Antibody Protein A Biotechnology SLPI medicine.drug |
Popis: | The large scale production of a monoclonal anti-progesterone antibody in serum free medium followed by affinity chromatography on protein G lead to a contamination of the antibody sample with a protein of about 14. kDa. This protein was identified by mass spectrometry as secretory leukocyte protease inhibitor (SLPI). This SLPI contamination lead to a failure of the fiber-optic based competitive fluorescence assay to detect progesterone in milk. Purification of the monoclonal antibody using protein A columns circumvented this problem. |
Databáze: | OpenAIRE |
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