By the same authors

From the same journal

Proteomic analysis of a Pleistocene mammoth femur reveals more than one hundred ancient bone proteins

Research output: Contribution to journalArticlepeer-review


  • Enrico Cappellini
  • Lars J Jensen
  • Damian Szklarczyk
  • Aurélien Ginolhac
  • Rute A R da Fonseca
  • Thomas W Stafford
  • Steven R Holen
  • Matthew J Collins
  • Ludovic Orlando
  • Eske Willerslev
  • M Thomas P Gilbert
  • Jesper V Olsen


Publication details

JournalJournal of Proteome Research
DateE-pub ahead of print - 21 Nov 2011
DatePublished (current) - 2011
Issue number2
Pages (from-to)917-926
Early online date21/11/11
Original languageEnglish


We used high-sensitivity, high-resolution tandem mass spectrometry to shotgun sequence ancient protein remains extracted from a 43,000 years old woolly mammoth (Mammuthus primigenius) bone preserved in the Siberian permafrost . For the first time, 126 unique protein accessions, mostly low-abundance extracellular matrix and plasma proteins, were confidently identified by solid molecular evidence. Among the best characterized was the carrier protein serum albumin, presenting two single amino acid substitutions compared to extant African (Loxodonta africana) and Indian (Elephas maximus) elephant. Strong evidence was observed of amino acid modifications due to post-mortem hydrolytic and oxidative damage. A consistent subset of this permafrost bone proteome was also identified in more recent Columbian Mammoth (Mammuthus columbi) samples from temperate latitudes, extending the potential of the approach described beyond sub-polar environments. Mass spectrometry-based ancient protein sequencing offers new perspectives for future molecular phylogenetic inference and physiological studies on samples not amenable to ancient DNA investigation. This approach therefore represents a further step into the on-going integration of different high-throughput technologies for identification of ancient biomolecules, unleashing the field of paleoproteomics.

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