Abstract
Acyl phosphatase has been extracted from horse muscle and purified. The purification procedure consisted of an acid extraction, a precipitation of foreign proteins, a ZnCl 2 precipitation and two subsequent steps on Chromatographic columns of CM-Sephadex C-25. The homogeneity of the final product was established by starch gel electrophoresis, polyacrylamide gel electrophoresis, gel filtration on Sephadex G-75, and ultracentrifugation. The molecular weight was determined by the sedimentation and the Archibald procedures, the complete amino acid composition by ion exchange chromatography. Acyl phosphatase hydrolytic activity on some compounds was studied.
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