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- W2589761520 abstract "The aim of this study was to test how the affinity of monoclonal antibodies, raised against a vaccine candidate, influences the results obtained in a quantitative antigen-specific enzyme-linked immunosorbent assay (ELISA). The vaccine candidate is a fusion protein consisting of the N-terminal parts of two bacterial cell surface proteins, Rib and Alpha-C. To determine binding protein (Rib or Alpha C) the plates were coated with Rib-N and Alpha C-N separately. The quantity of antibodies was determined in U/ml against a mouse serum standard. By dividing the values obtained for each monoclonal antibody in this antigen specific ELISA with the concentration of IgG for each of the hybridoma supernatants, the specific activity of each monoclonal antibody was determined and expressed as units (U)/µg monoclonal antibody. Kinetic parameters and affinity constants were then determined for the 5 Rib-N specific and 5 of the Alp-N specific antibodies by surface plasmon resonance (SPR), using a Biacore 3000 instrument. The monoclonal antibodies were captured by an anti-mouse antibody and the vaccine candidate was injected over the captured monoclonal antibody in different concentrations. The results showed that the same quantity of different monoclonal antibodies gave different results when quantified by the antigen specific ELISA. Furthermore, the results indicate that differences in affinity for the antigen explain the difference observed between the antibodies in the quantitative ELISA analysis. These results also show that studies like this are of importance for the understanding of what is measured in an ELISA. (Less)" @default.
- W2589761520 created "2017-03-03" @default.
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- W2589761520 date "2016-01-01" @default.
- W2589761520 modified "2023-09-24" @default.
- W2589761520 title "Impact of antibody-antigen affinity on quantitative analysis of antigen-specific serum IgG by ELISA" @default.
- W2589761520 hasPublicationYear "2016" @default.
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