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Nucleation of hydroxyapatite by bone sialoprotein.

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Hunter, G K, Goldberg, H A·1993·Proceedings of the National Academy of Sciences

Abstract

Bone sialoprotein (BSP) and osteopontin, the major phosphorylated proteins of mammalian bone, have been proposed to function in the initiation of mineralization. To test this hypothesis, the effects of BSP and osteopontin on hydroxyapatite crystal formation were determined by using a steady-state agarose gel system. At low calcium phosphate concentrations, no accumulation of calcium and phosphate occurred in control gels or gels containing osteopontin. Gels containing BSP at 1-5 micrograms/ml, however, exhibited a visible precipitation band and significantly elevated Ca + PO4 contents. By powder x-ray diffraction, the precipitate formed in the presence of BSP was shown to be hydroxyapatite. These findings suggest that bone sialoprotein may be involved in the nucleation of hydroxyapatite at the mineralization front of bone.

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Metadata

Authors
Hunter, G. K., & Goldberg, H. A.
Venue
Proceedings of the National Academy of Sciences
Published
1993-09-15
Volume
90
Issue
18
Pages
8562-8565
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2051849197
Cited by
665
References
0
FWCI
21.69
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Nucleation of hydroxyapatite by bone sialoprotein. https://app.cochat.ai/papers/10.1073/pnas.90.18.8562
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Hunter, G. K., & Goldberg, H. A. (1993). Nucleation of hydroxyapatite by bone sialoprotein. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.90.18.8562

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.