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Characterization of collagens from marine invertebrates
Hamraoui, L.; Gaill, F. (1997). Characterization of collagens from marine invertebrates, in: Biologie des sources hydrothermales profondes = Biology of deep-sea hydrothermal vents: Journées d'échanges du Programme DORSALES = DORSALES Workshop Roscoff 6-8 octobre 1997. Cahiers de Biologie Marine, 38(2): pp. 124
In: (1997). Biologie des sources hydrothermales profondes = Biology of deep-sea hydrothermal vents: Journées d'échanges du Programme DORSALES = DORSALES Workshop Roscoff 6-8 octobre 1997. Cahiers de Biologie Marine, 38(2)[s.n.][s.l.]. 111-149 pp., more
In: Cahiers de Biologie Marine. Station Biologique de Roscoff: Paris. ISSN 0007-9723, more
Peer reviewed article  

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Keyword
    Marine

Authors  Top 
  • Hamraoui, L.
  • Gaill, F.

Abstract
    Two types of collagens were described from hydrothermal vent annelids and vestimentiferans (Gaill et al., 1991; Gaill et al., 1995). The cuticle collagen is a long molecule (1.5-2.4 microm) constituting the protective layer of animals. The second type of collagen is similar to the vertebrate fibrillar collagen. It is known that the protective layers are determinant in the colonization of the hydrothermal environment (Tunnicliffe, 1991; Gaill, 1993) and we were interested in three of their characteristics 1) the collagen specificity of hydrothermal organisms, 2) the biochemical diversity of collagens from annelids and vestimentiferans, 3) the specific distribution of these collagens in vestimentiferan tissues. The comparison of interstitial and cuticular collagens from these organisms following Matsumura's methods (1972), which consists in categorizing collagens by their ratios of hydroxilic, hydrophobic and polar amino acids, shows that both families of interstitial and cuticular collagens differ in their biochemical composition. The analysis of this diversity brings new informations on annelid cuticular collagens. Peculiarly, it does not show any specific biochemical characteristic related to the hydrothermal environment, the thermal stability being the only original feature found to date in the collagens of hydrothermal vent organisms (Gaill et al., 1995). In contrast, the Riftia collagens appear to be original in their amino acid composition and are different not only from the vertebrate collagens but also from annelid cuticular and intertitial collagens.

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