Mass spectrometric characterization of human skin elastin peptides produced by proteolytic digestion with pepsin and thermitase.
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Schmelzer CE, Getie M, Neubert RH
Mass spectrometric characterization of human skin elastin peptides produced by proteolytic digestion with pepsin and thermitase.
J Chromatogr A. 2005 Aug 12;1083(1-2):120-6.
- PubMed ID
- 16078697 [ View in PubMed]
- Abstract
This study investigated peptides resulting from the digestion of human skin elastin with pepsin and thermitase. Characterization of the peptides was performed using two complementary mass spectrometric techniques; LC/ESI-ion trap and nano-ESI-qTOF MS. 155 different peptides were identified using a combined database based and de novo sequencing approach resulting in a total sequence coverage of 65.4% calculated on the basis of the precursor tropoelastin (accession number A32707). A potential hydroxylation was found in 29% of the recovered prolines. Furthermore, the absence of amino acids expressed by exon 26A could be confirmed. However, contrary to earlier studies, amino acids expressed by exon 22 seem to exist.