Natural murine interferon-gamma. Evidence for post-translational proteolytic processing.

摘要: Murine interferon-gamma (MuIFN-gamma), produced by the T-cell lymphoma, L12-R4, and stimulated with phorbol myristic acetate, was purified rat monoclonal antibodies AN-18.17.24. The product retained its biologic activity consisted of two proteins (Mr = 17,500 16,500), as determined sodium dodecyl sulfate-gel electrophoresis. Both species were found to be glycosylated, since their Mr values decreased 14,500 13,500 when producing cells in presence tunicamycin. Analysis intracellular secreted forms [35S] methionine revealed that MuIFN-gamma is synthetized a single peptide undergoes proteolytic cleavage during or after secretion. Peptide mapping reverse phase high pressure liquid chromatography showed indeed profile both very similar, suggesting degree homology primary structure. These results demonstrate molecular heterogeneity probably outcome processing