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Analysis of Bone “Collagen” Extraction Products for Radiocarbon Dating

Published online by Cambridge University Press:  09 February 2016

F Brock*
Affiliation:
Oxford Radiocarbon Accelerator Unit, Research Laboratory for Archaeology & the History of Art, University of Oxford, Dyson Perrins Building, South Parks Road, Oxford OX1 3QY, United Kingdom
V Geoghegan
Affiliation:
Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, United Kingdom
B Thomas
Affiliation:
Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, United Kingdom
K Jurkschat
Affiliation:
Department of Materials, University of Oxford, Begbroke Science Park, Begbroke Hill, Oxford OX5 1PF, United Kingdom
T F G Higham
Affiliation:
Oxford Radiocarbon Accelerator Unit, Research Laboratory for Archaeology & the History of Art, University of Oxford, Dyson Perrins Building, South Parks Road, Oxford OX1 3QY, United Kingdom
*
2Corresponding author. Email: fiona.brock@rlaha.ox.ac.uk.

Abstract

Archaeological bones are now routinely dated in many radiocarbon laboratories through the extraction of “collagen.” Methods for “collagen” extraction vary, and several laboratories now apply an ultrafiltration step after gelatinization to extract the higher molecular weight (usually >10 or 30kDa) fraction for dating, thereby removing low molecular weight contaminants. Ultrafiltration has been demonstrated to result in products that are easier to handle and have more acceptable C:N ratios, and in some instances can result in significantly improved (generally older) 14C dates when compared to non-ultrafiltered products from the same bone. Although it has been suggested that ultrafiltration removes potential contaminants such as short-chain degraded collagen and other peptides and amino acids, fulvic acids, and salts, there remains little published evidence to support this. This paper presents data from a pilot study investigating the most suitable techniques with which to study the products of the routine “collagen” extraction procedures employed at the Oxford Radiocarbon Accelerator Unit (ORAU) (modified Longin followed by ultrafiltration). The preliminary data demonstrates that the final product of “collagen” extraction at ORAU appears to be an aggregate consisting of a range of proteins of different molecular weights, including collagen, as well as some other organic matter and inorganic species. Ultrafiltration is removing some, but not all, of the <30kDa fraction from the samples. Further work to investigate the nature of this aggregate and how best to improve the efficiency of “collagen” extraction procedures is discussed.

Type
Articles
Copyright
Copyright © 2013 by the Arizona Board of Regents on behalf of the University of Arizona 

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