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Inorganic Pyrophosphatase Activity of Purified Bovine Pulp Alkaline Phosphatase at Physiological pH
M. Harada
Department of Oral Biochemistry, Matsumoto Dental College, Shiojiri 399-07, Japan
N. Udagawa
Department of Oral Biochemistry, Matsumoto Dental College, Shiojiri 399-07, Japan
K. Fukasawa
Department of Oral Biochemistry, Matsumoto Dental College, Shiojiri 399-07, Japan
B.Y. Hiraoka
Department of Oral Biochemistry, Matsumoto Dental College, Shiojiri 399-07, Japan
M. Mogi
Department of Oral Biochemistry, Matsumoto Dental College, Shiojiri 399-07, Japan
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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Journal of Dental Research, Vol. 65, No. 2,
125-127 (1986)
DOI: 10.1177/00220345860650020601
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