Interferon produced by mouse L-929 cells by incubation with poly(rI)·poly(rC) is known to be composed of a mixture of MuIFN-α and MuIFN-β. The α component was separated from the β species by affinity chromatography over a monoclonal anti-MuIFN-β agarose column and partially purified by gel filtration. MuIFN-α, prepared by this method was separated into at least five subspecies by chromatofocusing. The approximate pI values of these components are ⩾ 7.5, 6.5, 6.2, 5.9 and 5.6, respectively. Component 3 (pI 6.2) was the most prominent subspecies present in our MuIFN-α preparations, representing 40 to 50% of the total antiviral activity. Component 1 (pI ⩾ 7.5) which accounted for about 5% of the antiviral activity on mouse cells, differed in some properties from the other interferon subspecies. It showed a relatively high antiviral activity on heterologous cells and it was eluted from a Sephadex column after the other α subspecies. Furthermore, it showed a diminished binding to heparin as compared to the other MuIFN-α subspecies, indicating a lower affinity for polynucleotides.


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