Literature DB >> 27313979

Rapid and Accurate Identification of Animal Species in Natural Leather Goods by Liquid Chromatography/Mass Spectrometry.

Yukari Izuchi1, Tsuneo Takashima2, Naoya Hatano3.   

Abstract

The demand for leather goods has grown globally in recent years. Industry revenue is forecast to reach $91.2 billion by 2018. There is an ongoing labelling problem in the leather items market, in that it is currently impossible to identify the species that a given piece of leather is derived from. To address this issue, we developed a rapid and simple method for the specific identification of leather derived from cattle, horses, pigs, sheep, goats, and deer by analysing peptides produced by the trypsin-digestion of proteins contained in leather goods using liquid chromatography/mass spectrometry. We determined species-specific amino acid sequences by liquid chromatography/tandem mass spectrometry analysis using the Mascot software program and demonstrated that collagen α-1(I), collagen α-2(I), and collagen α-1(III) from the dermal layer of the skin are particularly useful in species identification.

Entities:  

Keywords:  collagen; labelling; product tracing; quality control

Year:  2016        PMID: 27313979      PMCID: PMC4894823          DOI: 10.5702/massspectrometry.A0046

Source DB:  PubMed          Journal:  Mass Spectrom (Tokyo)        ISSN: 2186-5116


  4 in total

1.  Identification and quantification of different species in animal fibres by LC/ESI-MS analysis of keratin-derived proteolytic peptides.

Authors:  Sara Paolella; Mariangela Bencivenni; Francesca Lambertini; Barbara Prandi; Andrea Faccini; Cinzia Tonetti; Claudia Vineis; Stefano Sforza
Journal:  J Mass Spectrom       Date:  2013-08       Impact factor: 1.982

2.  Peptide Profiling Using Matrix-Assisted Laser Desorption/Ionization-Time-of-Flight Mass Spectrometry for Identification of Animal Fibers.

Authors:  Yukari Izuchi; Mutsumi Tokuhara; Tsuneo Takashima; Kanya Kuramoto
Journal:  Mass Spectrom (Tokyo)       Date:  2013-08-02

3.  Covalent crosslinking between molecules of type I and type III collagen. The involvement of the N-terminal, nonhelical regions of the alpha 1 (I) and alpha 1 (III) chains in the formation of intermolecular crosslinks.

Authors:  W Henkel; R W Glanville
Journal:  Eur J Biochem       Date:  1982-02

4.  Species identification of archaeological skin objects from Danish bogs: comparison between mass spectrometry-based peptide sequencing and microscopy-based methods.

Authors:  Luise Ørsted Brandt; Anne Lisbeth Schmidt; Ulla Mannering; Mathilde Sarret; Christian D Kelstrup; Jesper V Olsen; Enrico Cappellini
Journal:  PLoS One       Date:  2014-09-26       Impact factor: 3.240

  4 in total

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