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The Complete Purification of Human Leucocyte Interferon
Author(s) -
BERG K.,
HERON I.
Publication year - 1980
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1980.tb00017.x
Subject(s) - interferon , size exclusion chromatography , molecular mass , biological activity , affinity chromatography , chemistry , antibody , chromatography , biochemistry , biology , immunology , in vitro , enzyme
Human leucocyte interferon (HuLeIF) has now for The first time been purified by a series of techniques involving precipitation, get filtration, and affinity chromatography wiih Cu‐chelate, blue dextran, and antibody. The two major species of HuLelF were idenlified 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 HuLeIFwere demonstrated with moleculur weights of 19,500, 20,900 and 22,130 daltons, representing 15% of the biological activity. Specific activity of pure interferon is 2–10° interferon units/mg protein. Recovery was about 50%, and the purification factor exceeded 350,000.