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  • Title: Inorganic pyrophosphatase activity of purified bovine pulp alkaline phosphatase at physiological pH.
    Author: Harada M, Udagawa N, Fukasawa K, Hiraoka BY, Mogi M.
    Journal: J Dent Res; 1986 Feb; 65(2):125-7. PubMed ID: 3003174.
    Abstract:
    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 greater than beta-glycerophosphate greater than phosphorylcholine greater than p-nitrophenylphosphate greater than 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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