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Resolution of human fibroblast interferon into 2 distinct classes by thiol exchange chromatography

, : Resolution of human fibroblast interferon into 2 distinct classes by thiol exchange chromatography. Archives of Virology 62(4): 323-332

Chromatography of crude and purified human fibroblast interferon on activated thiol Sepharose 4B yielded 2 classes of material exhibiting different stability to inactivation by mechanical stress. Interferon which bound to the gel accounted for 20-30% of recoverable activity, could be eluted with reducing agents and was unstable. Unbound material did not bind on subsequent rechromatography and was stable to shear forces. Leukocyte interferon did not bind, nor did fibroblast interferon treated with thiol blocking reagents. Peak eluted fractions had a specific activity of up to 107.9 units/milligram of protein, representing a 1700, fold purification.


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