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Phosphoprotein phosphatase activity of bovine intestinal alkaline phosphatase

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Summary

The phosphoprotein phosphatase activity of a commerical preparation of bovine intestinal alkaline phosphatase (EC 3.1.3.1.) was examined using phosvitin and dentine phosphoprotein as substrates. Over 90% and 70% of the phosphorus from dentine phosphoprotein and phosvitin were hydrolyzed in 2 h. The optimum pH of the enzyme for the dephosphorylation of phosvitin and dentine phosphoprotein was nearly 6. No protein phosphatase activity was observed when the alkaline phosphatases from bovine liver and pulp were investigated.

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Authors and Affiliations

  1. Department of Oral Biochemistry, Matsumoto Dental College, 399-07, Shiojiri, Japan

    M. Harada, B. Y. Hiraoka, K. Fukasawa & K. M. Fukasawa

Authors
  1. M. Harada
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  2. B. Y. Hiraoka
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  3. K. Fukasawa
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  4. K. M. Fukasawa
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Additional information

This investigation was supported by a grant from the Ministry of Education, Japan to M. H. We are also grateful to Miss Kayoko Yanagisawa for her technical assistance and for typing the manuscript.

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Harada, M., Hiraoka, B.Y., Fukasawa, K. et al. Phosphoprotein phosphatase activity of bovine intestinal alkaline phosphatase. Experientia 37, 547–548 (1981). https://doi.org/10.1007/BF01990040

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