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SDS-Polyacrylamide Gel Electrophoresis of Purified Human Leucocyte Interferon and the Antiviral and Anticellular Activities of the Different Interferon Species

The Institute of Medical Microbiology The Bartholin Building University of Aarhus, DK-8000 Aarhus C Denmark

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. 10⁹ 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).

Received 5 October 1979; accepted 16 May 1980.