Journal
ANALYTICAL BIOCHEMISTRY
Volume 374, Issue 2, Pages 325-334Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ab.2007.12.002
Keywords
bacterial collagenase; collagen; telopeptide; species variability; meat and bone meal; archaeology; gelatin; mass spectrometry
Funding
- NERC [NE/C511148/1] Funding Source: UKRI
- Natural Environment Research Council [NE/C511148/1] Funding Source: researchfish
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We present a novel method for the isolation and analysis of the bone collagen (I) alpha 2 chain carboxytelopeptide as a species biomarker. Conventional methods for the analysis and sequencing of mixtures of proteins and peptides commonly involve using the protease trypsin to cleave proteins present in the sample. However, in the study of collagen, these methods result in very complex mixtures of peptides that are difficult to analyze and the acquired results are not reproducible. Here we use bacterial collagenase (from Clostridium histolyticum) for its ability to cleave the highly unusual Gly-Xaa-Yaa repeating sequence of collagen, where Xaa usually is Pro and Yaa often is Hyp. Followed by a simple isolation step using a reverse phase solid phase extraction cartridge, the alpha 2 (I) chain carboxytelopeptide call be readily analyzed by matrix-assisted laser desorption/ionization-mass spectrometry (MALDI-MS) and the results can be used to distinguish between different species of origin. (C) 2007 Elsevier Inc. All rights reserved.
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