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Multiple forms of rat dentin phosphoproteins.

W T Butler, M Bhown, M T DiMuzio

    Archives of Biochemistry and Biophysics
    |August 1, 1983
    PubMed
    Summary

    Rat dentin phosphoproteins are heterogeneous, with highly phosphorylated (HP) and moderately phosphorylated proteins identified. Further analysis revealed distinct primary structures in dephosphorylated HP fractions, indicating variations in rat dentin phosphoprotein composition.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Dentin Matrix Proteins

    Background:

    • Previous research indicated rat dentin phosphoprotein heterogeneity.
    • Separation by ion-exchange chromatography yielded distinct fractions.
    • Characterization involved electrophoresis, gel chromatography, and amino acid/phosphate analysis.

    Purpose of the Study:

    • To further characterize the heterogeneous phosphoprotein fractions from rat dentin.
    • To elucidate the structural differences between highly phosphorylated (HP) and moderately phosphorylated proteins.
    • To investigate the primary structure of dephosphorylated HP components.

    Main Methods:

    • Ion-exchange chromatography for protein separation.
    • Polyacrylamide gel electrophoresis (PAGE) for molecular weight estimation.

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  • Amino acid and phosphate analysis.
  • Enzymatic dephosphorylation using bovine intestinal alkaline phosphatase.
  • QAE-Sephadex A-25 chromatography for separating dephosphorylated components.
  • N-terminal sequencing.

    • Main Results:

    • Three Alcian blue-staining bands observed on gradient gels (90-95,000 MW).
    • Two bands identified as highly phosphorylated proteins (HP) with >400 phosphoserine residues/1000, lacking valine, leucine, phenylalanine, arginine.
    • One band identified as a moderately phosphorylated protein with ~250 phosphoserine residues/1000, higher in glutamic acid and proline.
    • Dephosphorylated HP (dP-HP) showed two N-terminal sequences (Asp-Asp-Asp-Asn and Asp-Asp-Pro-Asn).
    • dP-HP separated into two components (dP-HP1, dP-HP2) with distinct amino acid compositions and primary structures.

    Conclusions:

    • Rat dentin contains at least two distinct classes of highly phosphorylated proteins with differing primary structures.
    • The heterogeneity extends to the dephosphorylated state, indicating variations in the protein backbone.
    • These findings contribute to understanding the complex composition of dentin phosphoproteins.