RT-PCR amplification of globin cDNAs in Riftia pachyptila (Vestimentifera) using degenerate primers derived from the amino acid sequences of Lamellibrachia
Bailly, X.; Zal, F.; Jollivet, D. (1997). RT-PCR amplification of globin cDNAs in Riftia pachyptila (Vestimentifera) using degenerate primers derived from the amino acid sequences of Lamellibrachia, 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. 112
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; e-ISSN 2262-3094, more
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| Authors | | Top |
- Bailly, X.
- Zal, F.
- Jollivet, D.
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| Abstract |
The deep-sea hydrothermal vent tubeworm Riftia pachyptila is associated with diffuse venting areas (2-25 degree C) of the East Pacific Rise and the Galapagos Rift. Such a species is known to lack a digestive tube and to feed upon nutrients provided by sulphide-oxidizing endosymbionts which are located inside a specialized organ, the trophosome. As a consequence, to exploit the rich source of chemical energy (ic. H sub(2)S) represented by the vent emissions, Riftia pachyptila has to cope with the alternation of acro-anaerobic conditions of the vent mixing which highly fluctuate with time. As such, Riftia pachyptila experiences transient but low levels of oxygen which impose peculiar respiratory adaptations, and also needs to transport hydrogen sulphide to the symbionts via a respiratory pigment, the haemoglobin. Indeed, the deep-sea tubeworm Riftia pachyptila possesses a multi-haemoglobin system with two different extracellular haemoglobins (Hbs) in the vascular blood, Vl and V2, the former exhibiting a typical annelid hexagonal bilayer (HBL) quaternary structure, and one extracellular Hb, Cl, in the coelomic fluid. These Hbs display a high oxygen affinity and a high cooperativity but have also the ability to bind sulphide reversibly with a high affinity. |
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