An aliquot of powder was hydrolysed directly (TB) for amino acid racemisation analysis.
Remaining bone powder was demineralised overnight in 1 M HCl (10 ml HCl per 500 mg bone powder).
In experimentally degraded bone, values for amino acid and elemental (C: N) composition, bulk δ N, and aspartic acid racemisation (AAR) changed very little until 99% of the collagen was lost, suggesting that the collagen triple helix and polypeptide chains remained remarkably intact.
30% of initial polymer length) which clearly persists in bone of considerable antiquity.
It is instructive to contrast the relative ease of ‘collagen’ purification with the difficulties encountered when )—to provide a ‘fingerprint’ of the molecular integrity of ancient collagen.
Measurements were made in relation to a reference (albumin) with known %C and %N and traceable to international V-PDB and AIR standards.
The analytical precision of isotopic determinations based on repeated measurements was better than 0.2‰ in both cases.