The effect of hydroxyapatite on the activity of alkaline and acid phosphatase was studied in a simple in vitro system. Alkaline phosphatase had a reduced activity in the absorbed state, and the pH-optimum for the adsorbed enzyme had decreased with one-half pH unit. The acid phosphatase was not influenced by the apatite in the presence of substrate. When no substrate stabilized the enzyme, a reduction was observed. This reduction was larger at pH values close to the pH-optimum for the enzyme.
Get full access to this article
View all access options for this article.
References
1.
James, L.K., and Augenstein, L.G. : Adsorption of Enzymes at Interfaces; Film Formation and the Effect on Activity, Adv in Enzym28, 1966.
2.
Danielli, J.F. : Cytochemistry; A Critical Approach, New York: John Wiley and Sons, Inc., 1936.
3.
Bradfield, J.R.G. : The Localization of Enzymes in Cells, Biol Rev Cambridge Phil Soc25:113-157, 1950.
4.
Bevelander, G.: Calcification of Mollusks: III. Intake and Deposition of "Ca and "P in Relation to Shell Formation, Biol Bull102:9-15, 1952.
5.
Sognnaes, R.F. , and Lustig, L.: Histochemical Reactions in the Lamprey Mouth , J Dent Res34:132-143, 1955.
6.
McDougal, V.: Adsorption from the Intestine, London: Longmans Green, 1936.
7.
Reith, D.J.: The Ultrastructure of Ameloblasts during Early Stages of Maturation of Enamel , J Cell Biol18:691-696, 1963.
8.
Chauncey, H.H. , and Quintarelli, G.: Histochemical Localization of Hydrolytic Enzymes in Human Salivary Glands, J Dent Res38:961-968, 1959.
9.
Burstone, M.S. : Histochemical Comparison of Naphtol AS-phosphates for the Demonstration of Phosphatases, J Natl Cancer Inst20:601-615, 1958.
