SDS-polyacrylamide gel electrophoresis of purified human leucocyte interferon and the antiviral and anticellular activities of the different interferon species

The Journal of General Virology
K Berg, I Heron

Abstract

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).

Citations

Jan 1, 1985·Pharmacology & Therapeutics·J A Langer, S Pestka
Aug 1, 1991·Veterinary Immunology and Immunopathology·M Abolhassani, K L Jacobsen
Feb 11, 2015·Biomedicine & Pharmacotherapy = Biomédecine & Pharmacothérapie·Kamaljeet KaurOm Prakash Katare
Sep 30, 1982·Biochimica Et Biophysica Acta·M Rubinstein
Jul 1, 1984·The Journal of Investigative Dermatology·J A Langer, S Pestka

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