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  • 1
    ISSN: 1430-3418
    Keywords: Deep sea ; Haemocyanin ; Hypoxia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The functional properties of the haemocyanin ofVampyroteuthis infernalis (Cephalopoda: Vampyromorpha), measured at 5 °C, are reported and discussed in relation to hypoxia. The oxygen affinity of this haemocyanin (P50=0.47−0.55 kPa) is higher than any previously measured for a cephalopod. The high cooperativity (n50=2.20−2.23) and Bohr coefficient (−0.22) suggest a true transport function for this haemocyanin. This high-affinity haemocyanin, in conjunction with moderate gill diffusion capacity, provides a sufficient oxygen gradient from the environment to the blood to support the low routine oxygen consumption rate of V. infernalis
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0887-3585
    Keywords: vestimentifera ; structure ; cryoelectron microscopy ; frozen-hydrated specimens ; single-particle 3D reconstruction ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: A frozen-hydrated specimen of the V1 hemoglobin of the hydrothermal vent tube worm Riftia pachyptila was observed in the electron microscope and subjected to three-dimensional reconstruction by the method of random conical tilt series. The 3D volume possesses a D6 point-group symmetry. When viewed along its 6-fold axis the vertices of its upper hexagonal layer are 16° clockwise rotated compared to those of the lower layer. A central linker complex is decorated by 12 hollow globular substructures. The linker complex comprises (i) a central hexagonal toroid, (ii) two internal bracelets onto which the hollow globular substructures are built, and (iii) six structures connecting the two hexagonal layers. The hollow globular substructures, related to the dodecamers of globin chains resulting from the dissociation of the hexagonal bilayer hemoglobin, have a local pseudo 3-fold symmetry and are composed each of three elongated structures visible when the volume is displayed at high threshold. At a resolution of 36 Å, the 3D volumes of the hexagonal bilayer hemoglobins of Riftia pachyptyla and of the leech Macrobdella decora look almost perfectly identical. © 1996 Wiley-Liss, Inc.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Publication Date: 2015-01-16
    Description: Siboglinids are symbiotic polychete annelids having hemoglobins as essential oxygen- and sulfide-carriers for their endosymbiotic bacteria. We analyzed the structure of the hemoglobins from two species of siboglinids: the monilifera Sclerolinum contortum and the frenulata Oligobrachia webbi (i.e. haakonmosbiensis) from Norwegian cold seeps. Measured by Multi-Angle Laser Light Scattering (MALLS), Sclerolinum shows a 3190 ± 50 kDa hexagonal bilayer hemoglobin (HBL-Hb) and a 461 ± 46 kDa ring-Hb, just as vestimentifera, whereas Oligobrachia has a 409 ± 3.7 kDa ring-Hb only. Electrospray Ionization-Mass Spectrometry (ESI-MS) showed Sclerolinum HBL-Hb composed of seven monomeric globins (15–16 kDa), three disulfide-bonded globin heterodimers and three linkers. The heterodimers always contain globin-b (15814.4 ± 1.5 Da). Sclerolinum ring-Hb is composed of globins and dimers with identical masses as its HBL-Hb, but lacks linkers. Oligobrachia ring-Hb has three globin monomers (14–15 kDa) only, with no disulfide-bonded dimers. Comparison of Sclerolinum hemoglobins between Storegga and Haakon Mosby Mud Volcano, using the normalized height of deconvoluted ESI-MS peaks, shows differences in globin monomers abundances that could reflect genetic differences or differential gene expression between distinct seep populations. The discovery of HBL-Hb in Sclerolinum is a new element supporting the hypothesis of monilifera being phylogenetically more closely related to vestimentifera, than to frenulata.
    Repository Name: EPIC Alfred Wegener Institut
    Type: Article , isiRev
    Format: application/pdf
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  • 4
    Publication Date: 2021-07-05
    Description: The functional properties of the haemocyanin ofVampyroteuthis infernalis (Cephalopoda: Vampyromorpha), measured at 5 °C, are reported and discussed in relation to hypoxia. The oxygen affinity of this haemocyanin (P50=0.47−0.55 kPa) is higher than any previously measured for a cephalopod. The high cooperativity (n50=2.20−2.23) and Bohr coefficient (−0.22) suggest a true transport function for this haemocyanin. This high-affinity haemocyanin, in conjunction with moderate gill diffusion capacity, provides a sufficient oxygen gradient from the environment to the blood to support the low routine oxygen consumption rate of V. infernalis.
    Type: Article , PeerReviewed
    Format: text
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