title: Partial purification and characterization of human gamma (immune) interferon.
abstract: Human gamma (immune) interferon (IFN-gamma) was produced in lymphocyte cultures stimulated with a phorbol ester (12-O-tetradecanoylphorbol 13-acetate) and purified phytohemagglutinin. Physicochemical analysis showed that human IFN-gamma is a glycoprotein with an isoelectric point around 8.6 and an apparent molecular weight of 58,000 +/- 3000. A purification process for IFN-gamma was developed consisting of sequential chromatographic separations on controlled-pore glass, concanavalin A-Sepharose, and Bio-Gel P-200. This purification process resulted in an increase in specific activity from about 10(4) (crude culture fluid) to an estimated 10(7) units per mg of protein with a cumulative recovery of about 40% of the IFN activity.
mesh_terms: D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D003208:Concanavalin A; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007372:Interferons / Q000096:biosynthesis / Q000302:isolation & purification*; D008214:Lymphocytes / Q000187:drug effects / Q000378:metabolism; D046911:Macromolecular Substances; D008970:Molecular Weight; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
chemical_list: D046911:Macromolecular Substances; D003208:Concanavalin A; D007372:Interferons; D013755:Tetradecanoylphorbol Acetate