Jitsukawa T, Nakajima S, Sugawara I, Watanabe H
Laboratory for Immunology, Hoechst Japan Limited, Saitama.
J Immunol Methods. 1989 Jan 17;116(2):251-7. doi: 10.1016/0022-1759(89)90211-1.
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.
三种针对重组干扰素-γ（rIFN-γ）的单克隆抗体（MAb）与固定在酶联免疫吸附测定（ELISA）板表面的rIFN-γ反应不佳。然而，当使用rIFN-γ和牛血清白蛋白（BSA）的混合物进行包被时，MAb与固定化rIFN-γ的结合显著增强。就抗原-抗体反应而言，这种增强是特异性的。这些结果表明，板塑料表面上rIFN-γ的量增加了，并且rIFN-γ的原始结构得以保留。
