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Phosphopeptides of Enamel Matrix

Department of Orthopaedic Surgery, Harvard Medical School, Children's Hospital Medical Center, Boston, Massachusetts 02115, U.S.A.

Although the tripeptides Glu-O-Phosphoserine-Tyr and Glu-O-Phosphoserine-Leu have been identified in embryonic bovine enamel proteins,^1,2 the issue of whether both sequences occur in each of the phosphopeptides, or whether certain sequences occur in specific peptides only, has recently been resolved by isolating homogeneous samples of E₃³ and E₄⁴. All three of the Ser residues of both peptides are phosphorylated. All three in E3 are in the sequence Glu-O-Phosphoserine-Leu, and all three in E₄ are in the sequence Glu-O-Phosphoserine-Tyr. It was not possible to sequence either of the polypeptide chains directly by automatic peptide sequencing. However, a partial sequence of E4 was constructed from data derived from peptides isolated after cyanogen bromide, trypsin and chymotrypsin digestions. The presence of Glu, Tyr and Leu adjacent to and near the O-Phosphoserine [Ser(L)] residues and the 2°, 3° and higher ordered structures of the enamel phosphopeptides may be important in calcium binding and mineralization.

Journal of Dental Research, Vol. 58, No. 2 suppl, 790-809 (1979)
DOI: 10.1177/00220345790580023101


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