1887

Abstract

SUMMARY

L cell interferon was purified by precipitation with zinc acetate and chromatography on DEAE- and CM-Sephadex, to a maximum sp. act. of 2 × 10 international 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 interferon 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 × 10 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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1974-04-01
2022-08-11
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