Increased coating efficiency of antigens and preservation of original antigenic structure after coating in ELISA.
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.
Jitsukawa
T
T
Laboratory for Immunology, Hoechst Japan Limited, Saitama.
Nakajima
S
S
Sugawara
I
I
Watanabe
H
H
D000911:Antibodies, Monoclonal / Q000276:immunology; D000937:Antigen-Antibody Reactions; D000941:Antigens / Q000276:immunology*; D004306:Dose-Response Relationship, Immunologic; D004797:Enzyme-Linked Immunosorbent Assay / Q000379:methods*; D000939:Epitopes; D007371:Interferon-gamma / Q000276:immunology*; D011485:Protein Binding; D011994:Recombinant Proteins; D012710:Serum Albumin, Bovine
D000911:Antibodies, Monoclonal; D000941:Antigens; D000939:Epitopes; D011994:Recombinant Proteins; D012710:Serum Albumin, Bovine; D007371:Interferon-gamma