title: The complete purification of human leucocyte interferon.
abstract: Human leucocyte interferon (HuLeIF) has now for the first time been purified by a series of techniques involving precipitation, gel filtration, and affinity chromatography with Cu-chelate, blue dextran, and antibody. The two major species of HuLeIF were identified as two clearly separable and stainable proteins representing 85% of the biological activity with molecular weights of 18,400 and 20,180 daltons. Three more subspecies of HuLeIF were demonstrated with molecular weights of 19,500, 20,900 and 22,130 daltons, representing 15% of the biological activity. Specific activity of pure interferon is 2 x 10(9) interferon units/mg protein. Recovery was about 50%, and the purification factor exceeded 350,000.
mesh_terms: D000915:Antibody Affinity; D011232:Chemical Precipitation; D002846:Chromatography, Affinity / Q000379:methods; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D006801:Humans; D007372:Interferons / Q000302:isolation & purification*; D007962:Leukocytes / Q000032:analysis*; D008970:Molecular Weight; D011506:Proteins / Q000032:analysis
chemical_list: D011506:Proteins; D007372:Interferons