The exposure of bovine enamel to an albumin-containing demineralizing solution results in penetration of protein into the porous enamel. Washing of this albumin-containing enamel results in a complete (low pretreatment albumin concentrations) or partial removal of the albumin (pretreatment concentrations ≧200 μg/ml-1). Subsequent exposure to increasing salt concentrations of fluoride, phosphate, calcium or chloride shows a partial removal of albumin at fluoride or phosphate concentrations of 75 mM while complete removal occurred at 150–200 mM fluoride or phosphate. Exposure to either calcium or chloride, even at 3 M concentrations, showed a negligible albumin release. It is proposed that protein removed at high fluoride or phosphate concentrations is bound by a strong interaction between protein-carboxyl groups and calcium on the surface of the enamel mineral. The partial removal of albumin released at low fluoride or phosphate concentrations indicates an enamel-albumin interaction by means of Ca-bridging between protein-carboxyl groups and mineral phosphates. Finally, it is suggested that salt-free washing removes albumin that has lost its native form upon binding to the partially dissolved crystallites of the enamel. It is concluded that enamel is mainly protected from demineralization by the inhibitory effects of protein penetrated into the pores, in addition to possible protection by the pellicle on the surface.

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