Modulation of crystal formation by bone phosphoproteins: structural specificity of the osteopontin-mediated inhibition of hydroxyapatite formation.

@article{Hunter1994ModulationOC,
  title={Modulation of crystal formation by bone phosphoproteins: structural specificity of the osteopontin-mediated inhibition of hydroxyapatite formation.},
  author={Graeme K. Hunter and Cam Kyle and Harvey A. Goldberg},
  journal={The Biochemical journal},
  year={1994},
  volume={300 ( Pt 3)},
  pages={723-8}
}
Osteopontin is a phosphorylated sialoprotein containing a conserved sequence of contiguous aspartic acid residues. This protein is expressed at high levels in mineralized tissues and has previously been shown to inhibit the in vitro formation of hydroxyapatite (HA). In the present study, protein modification and model compound studies have been used to identify the structural features of osteopontin that are responsible for its crystal-modulating properties. Using metastable calcium phosphate… CONTINUE READING
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