Mouse, hamster, rabbit, horse, and human interferons bind to immobilized Cibacron Blue F3GA under appropriate solvent conditions. Three forms of the immobilized ligand have been investigated: Cibacron Blue F3GA-Sepharose 4B, Blue Dextran-Sepharose 4B and Blue Sepharose CL-6B. The strength of binding of an interferon depends critically on the sorbent: Cibacron Blue F3GA-Sepharose 4B is the weakest in the series and Blue Sepharose CL-6B the strongest. The use of Blue Dextran-Sepharose 4B--a sorbent of intermediate binding properties--allows the complete separation of hamster, mouse and human fibroblast interferons in a single chromatographic step. Indeed, both the resolution, as well as the recovery, of those interferons is complete--regardless of the relative complexity of the chromatographed preparation (containing either crude or purified interferons). Thus, these ligands should prove of considerable use when a facile chromatographic evaluation, both qualitative and quantitative of mammalian interferons is required.
Syrian hamster interferon, produced by benzo(a)pyrene-transformed embryo cells does not display an affinity for Zn++ chelate-agarose. However, the interferon binds to Cu++ chelate-agarose and can be displaced from the column by a falling pH-gradient. The chromatography of crude hamster interferon preparation on a tandem of columsn: Zn++ chelate-agarose in equilibrium Cu++ chelate-agarose results in a 25-fold purification of interferon.
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