SDS-polyacrylamide gel electrophoresis of purified human leucocyte interferon and the antiviral and anticellular activities of the different interferon species.
Human leucocyte interferon (HuLeIF) was purified by a series of techniques involving precipitation, gel filtration, Cu-chelate-, blue dextran- and antibody-affinity chromatography. The two major species of HuLeIF were identified in SDS-PAGE as two clearly separable and stainable proteins representing 85% of the biological activity. Three more species of HuLeIF representing 15% of the biological activity were also demonstrated. The specific activity of pure interferon proteins was approx. 10(9) IFU/mg protein. Recovery was about 50% and the purification factor exceeded 350000. All five species of HuLeIF had definite anticellular activities when tested with Daudi cells (inhibition of thymidine uptake).
D002455:Cell Division / Q000187:drug effects; D002460:Cell Line; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007372:Interferons / Q000032:analysis* / Q000302:isolation & purification / Q000494:pharmacology; D008970:Molecular Weight; D014721:Vesicular stomatitis Indiana virus / Q000254:growth & development
D007372:Interferons