By the same authors

From the same journal

A method of isolating the collagen (I) alpha 2 chain carboxytelopeptide for species identification in bone fragments

Research output: Contribution to journalArticle

Author(s)

Department/unit(s)

Publication details

JournalANALYTICAL BIOCHEMISTRY
DatePublished - 15 Mar 2008
Issue number2
Volume374
Number of pages10
Pages (from-to)325-334
Original languageEnglish

Abstract

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.

    Research areas

  • bacterial collagenase, collagen, telopeptide, species variability, meat and bone meal, archaeology, gelatin, mass spectrometry, MASS-SPECTROMETRY, MITOCHONDRIAL-DNA, ANCIENT DNA, LATE-PLEISTOCENE, PCR DETECTION, ANIMAL FEED, I COLLAGEN, PROTEIN, MEAL, SEQUENCES

Discover related content

Find related publications, people, projects, datasets and more using interactive charts.

View graph of relations