Purification of Mouse Interferon by Affinity Chromatography on Anti-Interferon Globulin-Sepharose

Abstract

Mouse interferon produced in L cells was subjected to affinity chromatography on Sepharose-bound anti-interferon globulin. The hyperimmune anti-interferon serum was specifically adsorbed to remove antibodies against proteins derived from normal L cells, medium, and inducer virus preparation. The method permitted selective elimination of identified contaminant antigens from crude interferon preparations. Recovery of interferon was quantitative, and purification during this step was from 20- to 50-fold. Specific activities in peak fractions ranged from 1 to 2.7 × 10⁸ National Institutes of Health reference units per mg protein. Interferons induced by irradiated Newcastle disease virus and poly I:C were purified to the same degree.