Abstract
Abstract A phosphatase preparation was isolated from the electric organ of the eel with the enzyme properties of “acid phosphatases”. p -Nitrophenylphosphate and β-glycerophosphate were hydrolysed by this preparation at pH 5.0–5.5 and 38°. The enzyme was purified by the following procedures: aqueous extraction; absorption of contaminant proteins by tricalcium phosphate gel at pH 5.1; precipitation of the active fraction with 35–45% (NH 4 ) 2 SO 4 . The enzyme was inhibited by F − , and enhanced by EDTA. Na + , K + , Ca 2+ , Mg 2+ and p -chloromercuribenzoic acid had no effect. Phosphorylcholine, creatine phosphate and ATP were also hydrolysed by the preparation but at different rates and different pH's.
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