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Collagen proteins exchange oxygen with demineralisation and gelatinisation reagents and also with atmospheric moisture.

Accepted version
Peer-reviewed

Type

Article

Change log

Authors

von Holstein, Isabella CC  ORCID logo  https://orcid.org/0000-0002-2538-8457
von Tersch, Matthew 
Coutu, Ashley N 
Penkman, Kirsty EH 
Makarewicz, Cheryl A 

Abstract

RATIONALE: The oxygen (O) isotope composition of collagen proteins is a potential indicator of adult residential location, useful for provenancing in ecology, archaeology and forensics. In acidic solution, proteins can exchange O from carboxylic acid moieties with reagent O. This study investigated whether this exchange occurs during demineralisation and gelatinisation preparation of bone/ivory collagen. METHODS: EDTA and HCl demineralisation or gelatinisation reagents were made up in waters with different δ18 O values, and were used to extract collagen from four skeletal tissue samples. Aliquots of extracted collagen were exposed to two different atmospheric waters, at 120°C and ambient temperature, and subsequently dried in a vacuum oven at 40°C or by freeze drying. Sample δ18 O values were measured by HT-EA pyrolysis/IRMS using a zero-blank autosampler. RESULTS: Collagen samples exchanged O with both reagent waters and atmospheric water, which altered sample δ18 O values. Exchange with reagent waters occurred in all extraction methods, but was greater at lower pH. Damage to the collagen samples during extraction increased O exchange. The nature of exchange of O with atmospheric water depended on the temperature of exposure: kinetic fractionation of O was identified at 120°C but not at ambient temperature. Exchange was difficult to quantify due to the high variability of δ18 O values between experimental replicates. CONCLUSIONS: Studies of δ18 O values in collagen proteins should avoid extraction methods using acidic solutions.

Description

Keywords

0907 Environmental Engineering

Journal Title

Rapid Commun Mass Spectrom

Conference Name

Journal ISSN

0951-4198
1097-0231

Volume Title

32

Publisher

Wiley