title: Purification of chick interferon by zinc chelate affinity chromatography and sodium dodecylsulfate-polyacrylamide gel electrophoresis.
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.
authors.forename: U
authors.initials: U
authors.lastname: Krempien
authors.forename: I
authors.initials: I
authors.lastname: Redmann
authors.forename: C
authors.initials: C
authors.lastname: Jungwirth
mesh_terms: D000482:Allantois / Q000032:analysis; D000818:Animals; D002642:Chick Embryo; D002845:Chromatography / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D007372:Interferons / Q000302:isolation & purification*; D015032:Zinc
chemical_list: D007372:Interferons; D015032:Zinc