Physics
Scientific paper
Nov 1991
adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=1991e%26psl.107..380a&link_type=abstract
Earth and Planetary Science Letters, Volume 107, Issue 2, p. 380-388.
Physics
2
Scientific paper
Osteocalcin, a gamma-carboxyglutamic acid containing bone protein, is tightly bound to the hydroxyapatite matrix of bone, and as a consequence it is relatively more stable than the dominant protein, collagen. Its distribution in nature is limited to vertebrates. Osteocalcin and collagen have been isolated from modern and fossil bone samples of different organisms in different depositional environments for analysis of their δ13C, δ15N and 14C content. Whereas collagen is susceptible t aqueous weathering, hydrolysis, solubilization and removal, as well as contamination by soil amino acids or peptides, osteocalcin is more strongly bonded to the apatite matrix of the bone and hence less prone to loss or replacement by contaminants. We present evidence suggesting that osteocalcin may be a more suitable protein fraction for obtaining accurate 14C age estimates and/or δ13C and δ15N for paleodietary reconstruction from bone samples.
Ajie Henry O.
Hauschka Peter V.
Kaplan Isaac R.
Sobel Harry
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