The extraction of phosphoproteins from bovine dentin

I. R. Dickson, M. T. Dimuzio, D. Volpin, S. Ananthanarayanan, Arthur Veis*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

40 Scopus citations


The phosphoprotein obtained by the neutral pH tris buffer extraction of acetic acid demineralized bovine dentin has been compared with the phosphoprotein extracted directly during the neutral pH EDTA demineralization process. The phosphoproteins isolated by DEAE-cellulose chromatography from the neutral pH EDTA demineralization extract are not identical to those isolated by the same procedure from the dentin which had been subjected to acid demineralization. The two demineralization procedures yield phosphoproteins different in amino acid content and in presence of 260 nm UV absorbing moiety. Even after sequential acid demineralization, trisbuffer extraction and EDTA extraction, the residual dentin contains bound phosphoprotein. A peptide fragment containing both collagen and phosphoprotein moieties has been isolated following digestion and cleavage of the insoluble dentin collagen with cyanogen bromide. The acid demineralization process appears to be accompanied by degradation which removes both protein and non-protein components from the phosphoprotein.

Original languageEnglish (US)
Pages (from-to)51-61
Number of pages11
JournalCalcified Tissue Research
Issue number1
StatePublished - Dec 1 1975


  • Collagen
  • Dentin
  • Mineralization
  • Phosphoproteins

ASJC Scopus subject areas

  • Medicine(all)
  • Endocrinology


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