At physiological pH, the hydrolytic activity of purified bovine pulp alkaline phosphatase toward phosphorus compounds was observed to be in the order of inorganic pyrophosphate > β-glycerophosphate > phosphorylcholine > p-nitrophenylphosphate > glucose-6-phosphate. Optimum pH of the enzyme toward inorganic pyrophosphate was shown to be 8.5, with around 60% of the activity at pH 7.5. The activity was increased by the addition of Mg2+, but a different pattern of activation was observed between pH 7.5 and 8.5.
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