Abstract
Mouse interferon has been purified to homogeneity by two-step affinity chromatography. Two polypeptide bands were obtained on sodium dodecyl sulphate–polyacrylamide gel electrophoresis migrating at molecular weights 35,000 and 22,000, both having antiviral activity. The 35,000 but not the 22,000 band, also stained with periodic acid–Schiff. The specific activity was 8×109 of our laboratory units, corresponding to 2.4×109 NIH reference units.
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De Maeyer-Guignard, J., De Maeyer, E., Tovey, M. et al. Purification of mouse interferon by sequential affinity chromatography on poly(U)– and antibody–agarose columns. Nature 271, 622–625 (1978). https://doi.org/10.1038/271622a0
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DOI: https://doi.org/10.1038/271622a0
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