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Seven stable mouse hybridomas secreting monoclonal antibodies to human fibroblast beta interferon (IFN-beta) were isolated, all seven of which belonged to IgGl subclass and kappa type. While neutralizing the antiviral activity of human fibroblast IFN-beta, they failed to neutralized both that of human IFN-alpha and human IFN-gamma. These monoclonal antibodies neutralized the antiviral activity of human fibroblast IFN-beta but not that of human IFN-alpha and IFN-gamma. Two of the seven monoclonal antibodies, YSB-1 and YSB-2, showed particularly high neutralization titers in the ascitic fluid. Monoclonal antibodies were purified from cultures of hybridoma grown in a serum-free medium. The purified monoclonal antibodies, YSB-1(5 micrograms/ml) and YSB-2(1 microgram/ml), neutralized IFN-beta from 10EU/ml to 1EU/ml. Human fibroblast IFN-beta was purified to 3.5 X 10(7) IU/mg protein (1.0 X 10(8) IU/mg protein in the peak fraction) by the monoclonal antibody (YSB-2) affinity column chromatography, whereas human recombinant IFN-beta obtained from E.coli was also purified to 6.5 X 10(7) IU/mg protein (1.1 X 10(8) IU/mg protein in the peak fraction) by the monoclonal antibody (YSB-1) affinity column chromatography.
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