Effect of fluoride in the apatitic lattice on adsorption of enamel proteins onto calcium apatites.

The selective adsorption of enamel proteins onto crystalline calcium apatites having different specific surface areas and various degrees of fluoride substitution was investigated. The proteins were obtained from the outer (close to the ameloblast) layer of secretory enamel of porcine permanent incisors. The adsorption of the enamel proteins was not affected markedly by the variation of specific surface area of the hydroxyapatites used as adsorbents, but it was enhanced substantially with increasing fluoride content in the crystalline lattice. Through the use of SDS- and two-dimensional polyacrylamide gel electrophoresis, it was shown that the originally secreted amelogenin (25 kd) as well as 60-90-kd and 5-6-kd molecules adsorbed most selectively onto the hydroxyapatites and that additional moieties having 21-23-kd and 14-18-kd molecular masses commenced to adsorb onto the apatitic surfaces with increasing degrees of fluoride substitution in the lattice. In contrast, the 20-kd amelogenin, a product partially degraded from the 25-kd amelogenin, showed no significant adsorption, even onto the fluoridated apatites. These results suggest that the retention of proteinaceous matrix in the developing enamel might be affected by the nature of the forming crystals.