Abstract
Alkaline phosphatase from Escherichia coli (APEC) is not retained at 4°C on a metal-free tris(carboxymethyl)ethylenediamine (TED) column, but at 15°C the metalloenzyme becomes bound to the gel. Chromatography of phosphatase on metal-free TED gel indicates a decline in its enzymic activity and zinc content to about 26% and 40%, respectively. The activity of chromatographed APEC can be partially restored by addition of zinc ions, indicating that metal-free TED gel is capable of removing zinc ions from alkaline phosphatase.
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