Abstract
The bovine dentin matrix still contains some noncollagenous proteins after thorough extraction and decalcification. These have been obtained following digestion of the matrix by cyanogen bromide. Peptides containing non-collagenous portions were isolated by chromatography on diethylaminoethyl cellulose columns and fractionated on hydroxyapatite columns. Several fractions were obtained. The principal component was a complex between a highly-phosphorylated serine-aspartic acid-rich protein and a collagen peptide. These collagenous and non-collagenous moieties could not be separated from each other even under highly dissociative solvent conditions. After digestion with collagenase, the resulting phosphoprotein fraction still contained a few residues of hydroxyproline and hydroxylysine, and an enhanced content of proline, compared to the equivalent directly extractable phosphophoryn of the matrix. These data were interpreted as indicating that the phosphophoryn which is not extractable in 0.5M ethylenediaminetetraacetic acid is in fact covalently bound to some specific section of the matrix collagen. The covalent modification of the collagen matrix with highly acidic phosphoproteins may have an important role in the mineralization process.
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