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Kappa-elastin preparation

OB Olivier Bocquet
DT Dignê Tembely
DR Damien Rioult
CT Christine Terryn
BR Béatrice Romier
AB Amar Bennasroune
SB Sébastien Blaise
HS Hervé Sartelet
LM Laurent Martiny
LD Laurent Duca
PM Pascal Maurice
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EDP were prepared as described previously [25]. Briefly, insoluble elastin was prepared from bovine ligamentum nuchae by hot alkali treatment. Purity was assessed by comparing its amino acid composition to the one predicted from the elastin gene product. Soluble EDP were then obtained from insoluble elastin as described [25]. The obtained mixture of EDP, termed kappa-elastin (κE), has been shown to contain several peptides harboring the bioactive GxxPG motifs [16]. Composition of EDP from κE was compared to EDP obtained after proteolysis of human elastin by neutrophil elastase by mass spectrometry analysis and shown to contain similar peptides harboring the bioactive GxxPG motif [16]. In addition, κE has been shown to exhibit the same biological properties as elastin hydrolysates obtained by human neutrophil elastase [16, 46].

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