Abstract
One of the most abundant noncollagenous proteins of dentin is a phosphoprotein rich in aspartic acid and phosphoserine. This protein occurs in soluble and inextractable forms, the latter being associated with the insoluble collagenous matrix. This protein is capable of tightly binding a relatively high level of calcium. Biosynthetic and radioautographic data suggest that shortly after its biosynthesis, the phosphoprotein is transported and bound to the collagen at the predentin-dentin junction. This event is probably central to the mineralization process, though other glycoproteins may be involved.
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