1887

Abstract

Summary

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 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).

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/content/journal/jgv/10.1099/0022-1317-50-2-441
1980-10-01
2019-11-17
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http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-50-2-441
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