Abstract
Recombinant human IFN α 2b coupled to a silica support was used for the purification of the IFN α-binding proteins from placental cell membrane extracts. The 100-kDa (p100) and 64-kDa (p64) proteins, which bind preferentially to an IFN α 2b-silica matrix, were identified. Using a monoclonal antibody (A6) against IFN-γR1, it was able to isolate p100 and p70, but only if IFN α 2b was present during chromatography. Similar interactions were observed using polyclonal antibody anti-IFN γ binding proteins, as assayed in Western blot. These interactions were identified as conformation dependent. We speculate that IFN α 2b receptor complex shares an IFN γ receptor complex epitope.
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