Testing the aminostratigraphy of fluvial archives: the evidence from intra-crystalline proteins within freshwater shells.
Until recently few studies of amino acid racemization of fossil bivalves and gastropods collected from river terrace deposits in Europe were based on the analysis of the intra-crystalline fraction. Instead they were based on the epimerization (racemization) of a single amino acid, isoleucine, and its inter-conversion to alloisoleucine. This paper presents data from the analysis of the intra-crystalline fraction of the shells, using a preparation technique of sample bleaching to remove the leachable matrix, thus leaving a component that exhibits closed-system behaviour. Reverse-phase HPLC separation with fluorescence detection allows the interpretation of four amino acids in detail: aspartic acid, glutamic acid, alanine and valine. The intra-crystalline fraction offers greater potential for improved resolution, especially when combined with the analysis of multiple amino acid d/l values, which racemize at different rates. This is explored using three species of freshwater gastropods (Bithynia tentaculata and troschelii, Valvata piscinalis) and the bivalve Corbicula. Sites of different ages within the Lower Thames river terrace sequence are used as a stratigraphical framework, with samples from other southern UK sites providing supplementary evidence. The results indicate better resolution using the intra-crystalline fraction over that obtained using unbleached shells, with differentiation possible at sites of up to MIS 7 age. However, for older sites, although values are always higher, the separation is less successful. A species effect has been identified between the gastropod shells. Despite the analysis of intra-crystalline protein, amino acid data from Corbicula remain problematical. Preliminary data on the opercula from Bithynia indicate that better resolution is possible, particularly at older sites.
Penkman
K E H
KE
BioArch, Departments of Biology, Archaeology and Chemistry, Biology S Block, University of York, P.O. Box 373, York YO10 5YW, UK.
Preece
R C
RC
Keen
D H
DH
Maddy
D
D
Schreve
D C
DC
Collins
M J
MJ
Science. 1990 Apr 6;248(4951):60-4
17843317
Quat Geochronol. 2008 Feb;3(1-2):2-25
19684879
Quat Int. 2010 Dec 1;228(1-2):25-37
21217810
Adv Protein Chem. 1965;20:37-107
5334827