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Human lymphoblastoid interferon was produced on an 800-liter scale (2.6 X 10(9) units) by induction of Namalva cells with Newcastle disease virus, strain B1. The interferon was partially purified by anti-leukocyte interferon affinity chromatography, sulfopropyl Sephadex ion exchange chromatography, isoelectric focusing, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Recovery of interferon after gel electrophoresis varied from 11 to 33% based on the original crude material, with about 35,000-fold purification. The gel electrophoresis resolved the antiviral activity into two components with apparent molecular weights of 18,000 and 22,000; treatment with glycosidases resulted in all the activity being associated with the lower molecular weight species. Interferon activity could be completely (85 to 113%) recovered from the gels by elution into a buffer containing sodium dodecyl sulfate. The presence of sodium dodecyl sulfate did not appear to affect the assay of interferon. The protein could also be completely (75 to 106%) eluted from gels stained with coomassie blue, again with no loss in activity.
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