Abstract
A hybrid murine myeloma (2-13F5) secreting a monoclonal antibody that specifically bound and neutralized murine interferon beta has been isolated. Affinity chromatography with immobilized 2-13F5 monoclonal antibody of murine IFN (containing both IFN-alpha and IFN-beta) separated an IFN-beta preparation that demonstrated one band with Coomassie Brilliant Blue staining of SDS-PAGE at a molecular weight of 35000 and a specific activity of 4.3 x 10(8) units/mg of protein. This monoclonal antibody neither bound nor neutralized murine IFN-alpha. In addition, it bound only 87% of the interferon demonstrating a molecular weight of 35K. Possible explanations of this partial binding are discussed.