Summary
The single phosphoprotein of fetal calf dentin, having a molecular weight of approximately 94,000 and a phosphorus content of 8% (w/w), was examined by31P NMR spectroscopy. The single resonance at 3.7 ppm at pH 10 and its chemical shift during acid titration established the phosphomonoester nature of the organic phosphorus moiety. During titration of the phosphoprotein with CaCl2 in the presence of inorganic orthophosphate ions, line broadening for the orthophosphate resonance was both phosphoprotein- and calcium-dependent, indicating ternary complex formation. The data indicate that the phosphoprotein of fetal calf dentin binds both calcium and inorganic orthophosphate ions and therefore has the requisite physical chemical properties necessary for it to facilitate the heterogeneous nucleation of a Ca-PO4 solid phase from solution during tissue mineralization.
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Lee, S.L., Veis, A., Glonek, T.: Dentin phosphoprotein: an extracellular calciumbinding protein, Biochemistry 16:2971–2979, 1977.
Zanetti, M., de Bernard, B., Linde, A.: Ca2+-binding studies of the phosphoprotein from rat-incisor dentine, Eur. J. Biochem. 113:541–545, 1981.
Weinstock, M., Leblond, C.P.: Radioautographic visualization of the deposition of a phosphoprotein at the mineralization front in the dentin of the rat incisor, J. Cell Biol. 56:838–845, 1973.
Lee, S.L., Kossiva, D., Glimcher, M.J.: Phosphoproteins of bovine dentin: Evidence for polydispersity during tooth maturation, Biochemistry, in press.
Glonek, T., Kleps, R.A., Griffith, E.J., Myers, T.C.: Phosphorus-31 nuclear magnetic resonance studies on condensed phosphates. I. Some factors influencing the phosphate middle group chemical shift, Phosphorus 5:157–164, 1975.
Glonek, T., Wange, P.J., Van Wazer, J.R.: Phosphorus-31 spin-lattice relaxation. 2. Inorganic ring and chain phosphates, J. Am. Chem. Soc. 98:7968–7973, 1976.
Glonek, T., Marotta, S.F.:31P magnetic resonance of intact endocrine tissue: adrenal glands of dogs, Horm. Metab. Res. 10:420–424, 1978.
Veis, A., Spector, A.R., Zamoscianyk, H.: The isolation of an EDTA-soluble phosphoprotein from mineralizing bovine dentin, Biochim. Biophys. Acta 257:404–413, 1972.
Sharkey, M.A., Veis, A.: Identification of a nucleotide conjugated to dentinal phosphoprotein, J. Dent. Res. 53 (special issue):57, 1974.
Glimcher, M.J.: Specificity of the molecular structure of organic matrices in mineralization. In R.F. Sognnaes (ed.): Calcification in Biological Systems, pp. 421–487. Am. Acad. Adv. Sci., Washington, DC, 1960.
Glimcher, M.J., Krane, S.M.: The organization and structure of bone, and the mechanism of calcification. In B.S. Gould, G.N. Ramachandran (eds.): Treatise on Collagen, vol. IIB, pp. 68–251. Academic Press, New York, 1968.
Glimcher, M.J.: Composition, structure, and organization of bone and other mineralized tissues and the mechanism of calcification. In R.O. Greep, E.B. Astwood (eds.): Handbook of Physiology 7: Endocrinology, vol. 7, pp. 25–116, Am. Physiological Soc., Washington DC, 1976.
Reeves, R.F., Latour, N.G.: Calcium phosphate sequestering phosphopeptide from casein, Science 128:172, 1958.
Glimcher, M.J.: On the form and function of bone: From molecules to organs. Wolff's Law revisited, 1981. In A. Veis (ed.): The Chemistry and Biology of Mineralized Tissues, pp. 618–673. Elsevier/North Holland, New York, 1981.
Veis, A., Stetler-Stevenson, W., Takagi, Y., Sabsay, B., Fullerton, R.: The nature and localization of the phosphorylated proteins of mineralized dentin. In A. Veis (ed.): The Chemistry and Biology of Mineralized Connective Tissues, pp. 377–387, Elsevier/North Holland, New York, 1981.
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Lee, S.L., Glonek, T. & Glimcher, M.J. 31P nuclear magnetic resonance spectroscopic evidence for ternary complex formation of fetal dentin phosphoprotein with calcium and inorganic orthophosphate ions. Calcif Tissue Int 35, 815–818 (1983). https://doi.org/10.1007/BF02405129
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DOI: https://doi.org/10.1007/BF02405129