Purification of mouse interferon by sequential affinity chromatography on poly(U)– and antibody–agarose columns (original) (raw)

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• Published: 16 February 1978

Nature volume 271, pages 622–625 (1978)Cite this article

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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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Authors and Affiliations

1. Institut du Radium, Bâtiment 110, Université de Paris-Sud, Orsay, 91405, France
   Jaqueline De Maeyer-Guignard & E. De Maeyer
2. Institut de Recherches Scientifiques sur le Cancer, 94800, Villejuif, France
   M. G. Tovey & I. Gresser

Authors

1. Jaqueline De Maeyer-Guignard
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2. E. De Maeyer
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3. M. G. Tovey
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4. I. Gresser
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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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• Received: 24 October 1977
• Accepted: 19 December 1977
• Issue Date: 16 February 1978
• DOI: https://doi.org/10.1038/271622a0

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