Adsorption of Bovine Serum Albumin and Porcine Enamel Proteins onto Carbonatoapatites: Effects of Adsorbent Composition and Magnesium Ion in Solution.

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The composition of enamel mineral corresponds to that of a calcium carbonatoapatite. In order to elucidate the regulatory mechanism of enamel mineralization through crystal-matrix protein interaction, we investigated the adsorption of bovine serum albumin and pig enamel proteins onto 24 batches of carbonatoapatites that were characterized with respect to their composition and properties. The adsorbents used were categorized into 2 groups: the calcium apatites precipitating at neutral pH incorporated the carbonate into both the hydroxyl (A-type) and phosphate ion (B-type) sites in their lattice, whereas the preparations made at the alkaline pH (high OH--CO32- competition) or in the presence of fluoride (F-CO32- competition) yielded only the B-type carbonatoapatite. Adsorption experiments yielded data showing that the adsorption behaviour of both adsorbates was markedly affected by the incorporation of ionic species (CO3, F, and Mg) into the crystal lattice and in the presence of Mg ion in the equilibrating solution. In these experiments, we also ascertained that no significant changes occurred in the composition or properties of the adsorbent during equilibration. The results obtained support the theory that any compositional changes in enamel mineral can modulate the crystal-protein interaction in situ. In this connection, it is pertinent that magnesium is one of the key players in the normal regulation and pathogenesis of enamel mineralization because the adsorption and lattice substitution of the ion can mediate the attenuation of protein adsorption onto carbonatoapatites, as well as the inhibition of apatite crystal growth.
歯科基礎医学会の論文

Adsorption of Bovine Serum Albumin and Porcine Enamel Proteins onto Carbonatoapatites: Effects of Adsorbent Composition and Magnesium Ion in Solution.

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歯科基礎医学会 | 論文

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