Abstract
Zinc chelated by iminodiacetic acid linked to an insoluble matrix binds human fibroblast interferon quite selectively at neutral pH in 0.15 M NaCL. On reduction of the pH and increase of the ionic strength, the interferon is eluted. Using a pH gradient at constant high ionic strength, good purification of the interferon can be obtained, up to a final specific activity of 108.5 units/mg of protein. Approximately 60% of the applied activity can be recovered.
Highlights
Zinc chelated by iminodiacetic acid linked to an insoluble matrix binds human fibroblast interferon quite selectively at neutral pH in 0.15 M NaCl
Metal chelate affinity chromatography is a recently reported technique [5,6,7] which depends on the binding of proteins at about neutral pH to zinc or copper ions immobilized by chelation on an insoluble matrix
The crude interferon preparation used in the experiments described here contained 104.6units/ml, with a protein concentration of 0.39 mglml
Summary
Zinc chelated by iminodiacetic acid linked to an insoluble matrix binds human fibroblast interferon quite selectively at neutral pH in 0.15 M NaCl. The crude interferon preparation used in the experiments described here contained 104.6units/ml, with a protein concentration of 0.39 mglml. It has been shown that fibroblast and leukocyte interferons have different dose-response curves [12, 13]; as the reference standard for human interferon is leukocyte-derived, it is not valid to express tibroblast interferon titers in terms of the standard reference unit.
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