Abstract
Summary
The pyro- and alkaline phosphatase activities of quail bone appear to be catalyzed by a single enzyme. The activities could not be separated after ion-exchange chromatography or gel filtration. The pH optima for pyro- and alkaline phosphatase were 8.0 and 10.7, respectively. Alkaline phosphatase activity was stimulated by magnesium. Optimal stimulation of pyrophosphatase activity occurred at a pyrophosphate to magnesium ratio of 2.5. Both enzymatic activities were not markedly affected by high concentrations of fluoride.
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