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  • Title: Purification of chick interferon by zinc chelate affinity chromatography and sodium dodecylsulfate-polyacrylamide gel electrophoresis.
    Author: Krempien U, Redmann I, Jungwirth C.
    Journal: J Interferon Res; 1985; 5(1):209-14. PubMed ID: 2580920.
    Abstract:
    An improved purification method for chick interferon from the allantoic fluid of embryonated chick eggs is described. Interferon prepurified by perchloric acid treatment, zinc acetate precipitation, and chromatography on SP-Sephadex C-25 was further enriched by column chromatography on zinc chelate. Analysis on sodium dodecylsulfate polyacrylamide gel electrophoresis of the interferon preparation with a specific activity of 8 X 10(5) units/mg protein shows that the major antiviral activity migrated in a broad band in the range of 20-29 kD molecular weight. Several protein bands were stainable with Coomassie blue and silver nitrate in this molecular weight range. Between 80 and 95% of the total protein charged to the gel could be removed from the interferon containing fractions by sodium dodecylsulfate polyacrylamide gel electrophoresis.
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