Electrophoretic Characterization of Purified Mouse L Cell Interferon of High Specific Activity

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Abstract
SUMMARY L cell interferon was purified by precipitation with zinc acetate and chromato- graphy on DEAE- and CM-Sephadex, to a maximum sp. act. of 2 x io s inter- national units per mg protein. As analysed by polyacrylamide gel electrophoresis, such preparations contained large amounts of contaminating proteins, some of which coincided in mobility with components in the corresponding material from uninduced L cell cultures. However, at the position of the dominant, sharp inter- feron peak, a protein band was discernible which was not apparent in the control material. The sp. act. of the electrophoretic peak interferon must be 3 x io s units, or more, per mg protein, and it appears that only several molecules, at the most, of interferon need be bound to a cell to exert a demonstrable antiviral action.

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