Journal of Archaeological Method and Theory

, Volume 19, Issue 3, pp 407–439

An Optimized Approach for Protein Residue Extraction and Identification from Ceramics After Cooking

Article

DOI: 10.1007/s10816-011-9120-5

Cite this article as:
Barker, A., Venables, B., Stevens, S.M. et al. J Archaeol Method Theory (2012) 19: 407. doi:10.1007/s10816-011-9120-5

Abstract

Extraction of protein residues from archaeological matrices, such as pottery clay, lithics, and grinding stones, has proven to be methodologically challenging. Protein residue analysis is fraught with technical challenges in analytical chemistry. In cooking pottery, protein residues are thought to bind to clay surfaces in vessel walls through a variety of primarily non-covalent interactions. Removal of protein residues requires the disruption of these interactions, and a diverse set of tools has been proposed and applied. Here, we test extraction procedures through varying combinations of physical parameters and solvents to derive an optimal approach yielding efficiencies of recovery from experimental pottery above 60%. The utility of our extraction approach was further validated through liquid chromatography–mass spectrometry analysis of experimental residues. We have identified several hurdles to developing a successful study of protein residues from pottery, each of which is surmountable with additional method development in the realm of archaeological chemistry.

Keywords

Archaeological chemistry Protein residues Paleodiet Method development 

Supplementary material

10816_2011_9120_MOESM1_ESM.xlsx (37 kb)
Tables A2–A5Homology reports for a selected group of proteins identified in this study. Identified peptides (rows) are compared against different proteins (columns) to determine which potential match is best. Listed values represent peptide identification probability. A2. Myosin-2. In this case, the variety of peptides allowed for the identification of the protein as myosin-2 from S. scrofa. A3. Phaseolin α. With only two possible candidates available (phaseolin α and β), the identification of this protein as being from Phaseolus is straightforward. A4. Actin. Although identified as actin, no clear species assignment could be made in this case due to extensive homology across diverse taxa. A5. Tropomyosin, β-chain. The potential source of these peptides includes primarily mammalian species (Homo sapiens, Mus musculus, Rattus norvegicus, Oryctolagus cuniculus, and Bos taurus), but the relatively low number of peptides identified makes specific assignment difficult (XLSX 37.3 kb)

Copyright information

© Springer Science+Business Media, LLC 2011

Authors and Affiliations

  • Andrew Barker
    • 1
    • 2
  • Barney Venables
    • 2
  • Stanley M. StevensJr.
    • 3
  • Kent W Seeley
    • 3
  • Peggy Wang
    • 2
  • Steve Wolverton
    • 1
  1. 1.Department of Geography, Center for Environmental ArchaeologyUniversity of North TexasDentonUSA
  2. 2.Department of Biological Science, Institute of Applied SciencesUniversity of North TexasDentonUSA
  3. 3.Department of Cell Biology, Microbiology, and Molecular BiologyUniversity of South FloridaTampaUSA

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