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Increased coating efficiency of antigens and preservation of original antigenic structure after coating in ELISA
T Jitsukawa1, S Nakajima, I Sugawara
1Laboratory for Immunology, Hoechst Japan Limited, Saitama.
Three monoclonal antibodies (MAbs) to recombinant interferon-gamma (rIFN-gamma) did not react well with rIFN-gamma immobilized on the ELISA plate surface. However, binding of the MAbs to immobilized rIFN-gamma was remarkably enhanced when a mixture of rIFN-gamma and bovine serum albumin (BSA) was used for coating. This enhancement was specific in terms of the antigen-antibody reaction. These results suggest that the amount of rIFN-gamma on the plate's plastic surface is increased and that the original structure of rIFN-gamma is preserved.
Three monoclonal antibodies (MAbs) to recombinant interferon-gamma (rIFN-gamma) did not react well with rIFN-gamma immobilized on the ELISA plate surface. However, binding of the MAbs to immobilized rIFN-gamma was remarkably enhanced when a mixture of rIFN-gamma and bovine serum albumin (BSA) was used for coating. This enhancement was specific in terms of the antigen-antibody reaction. These results suggest that the amount of rIFN-gamma on the plate's plastic surface is increased and that the original structure of rIFN-gamma is preserved.