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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 543 (1988), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-1793
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Sulfur content and fine structure were studied for tissues of three species of clams, Lucinoma annulata, Calyptogena elongata and Lucina floridana, which inhabit sulfide-rich environments and whose gills harbor symbiotic sulfur bacteria. Lucinoma annulata and C. elongata were dredged from the Santa Barbara basin, California, USA, at a depth of 480 to 490 m, and Lucina floridana were dug from below the roots of seagrasses in Saint Joseph Bay, Florida, at a depth of 0.25 to 2m. Foot tissue of Lucinoma annulata, without symbionts, had a total sulfur content of 1.4±0.1 (SD) mg 100 mg-1 dry weight of tissue (%DW). The symbiont-containing gill tissue of different individuals of L. annulata varied in color from dark red to pale yellow, and the total sulfur content was 2.5±0.4% DW in red gills and was 5.6±3.3 % DW in the yellowest gills. Maintenance of L. annulata in the laboratory for 21 d in the absence of sulfide resulted in the loss from the gill of yellow deposits which were elemental sulfur in the form of liquid-crystalline sulfur globules rather than solid orthorhombic sulfur crystals. The foot tissue did not contain elemental sulfur. When examined by freeze-etch microscopy, sulfur globules were found only within bacteria and not in the animal host cytoplasm. Sulfur globules were confined to the periplasmic space of the bacteria. C. elongata and Lucina floridana resembled Lucinoma annulata in the physical form and distribution of elemental sulfur. The absence of elemental sulfur in the animal cytoplasm suggests that its formation from sulfide is not a detoxification scheme to protect animal tissue from sulfide toxicity. The sulfur deposits probably represent inorganic energy reserves that permit the symbiotic bacteria to function even during the temporary absence of external sulfide.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 41 (1985), S. 1052-1054 
    ISSN: 1420-9071
    Keywords: Cardiac muscle ; phylogenesis ; sarcoplasmic reticulum ; phospholamban ; protein kinase ; Ca2+-transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Phospholamban, a sarcoplasmic reticulum phosphoprotein, is present in the hearts of mammalian, avian, amphibian, and fish species. Phylogenetic changes are indicated by marked differences among species in cardiac phospholamban content and by the absence of Ca2+/calmodulin-dependent phospholamban phosphorylation at an early developmental stage.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Marine biology 103 (1989), S. 291-302 
    ISSN: 1432-1793
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Hydrogen sulfide is a potent inhibitor of aerobic respiration. Sulfide is produced in sediments, and many species of fish live in association with the bottom. Tolerance tests, enzyme assays, and chromatography of sulfur compounds in thirteen species of shallow-water marine fishes (collected in San Diego, California, USA in 1987–1988) indicate adaptations to sulfide that vary with habitat and lifestyle. Tidal-marsh inhabitants, like Gillichthys mirabilis and Fundulus parvipinnis, have higher tolerance to sulfide (96 h LC50 at 525 to 700 μM) relative to outer-bay and open-coast inhabitants (surviving 〈12 h at much lower concentrations). The cytochrome c oxidase of all species shows high activity and susceptibility to sulfide poisoning, with 50% inhibition at 30 to 500 nM in various tissues. The two marsh species are able to survive at sulfide concentrations already inhibitory to their cytochrome c oxidase and fatal to other species. All species detoxify sulfide by oxidizing it to thiosulfate. All have sulfide-oxidizing activity in the blood, spleen, kidney, liver and gills, which correlates significantly with heme content. Thiosulfate appears in the tissues of sulfide-exposed fish and builds up to high concentrations (up to 2 mM) with stronger and longer exposure. Unexposed fish contain little or no thiosulfate. Sulfide is barely detectable in the tissues, even in high-sulfide exposure tests. We suggest that fish blood, in having high sulfide-oxidizing activity and no cytochrome c oxidase, can act as a short-term first line of defense against sulfide, and thus minimize the amount that reaches the vital organs. The results of this study indicate that sulfide is a significant environmental factor influencing the ecological distribution of marine fishes.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1432-1793
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The biological community that surrounds the hypersaline cold water brine seeps at the base of the Florida Escarpment is dominated by two macrofaunal species: an undescribed bivalve of the family Mytilidac and a vestimentiferan worm, Escarpia laminata. These animals are apparently supported by the chemoautotrophic fixation of carbon via bacterial endosymbionts. Water column and sediment data indicate that high levels of both sulfide and methane are present in surface sediments around the animals but absent from overlying waters. Stable isotopic analyses of pore water indicate that there are two sources of sulfide: the first is geothermal sulfide carried in groundwater leaching from the base of the escarpment, and the second is microbial sulfide produced in situ. The vestimentiferan E. laminata, and the mytilid bivalve (seep mussel) live contiguously but rely on different substrates for chemoautotrophy. Enzyme assays, patterns of elemental sulfur storage and stable isotopic analyses indicate that E. laminata relies on sulfide oxidation and the seep mussel on methane oxidation for growth.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1573-4919
    Keywords: heart ; sarcolemma ; phosphatidylethanolamine N-methylation ; cyclic AMP ; protein phosphorylation ; S-adenosyl-L-methionine ; neutral lipid methylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Premethylation of purified porcine cardiac sarcolemma (SL) in the presence of 0.15, 10 and 150 µM S-adenosyl-L-methionine (AdoMet) did not change the phosphorylation of SL proteins catalyzed either by intrinsic cyclic AMP-dependent protein kinase (cAK) or by added catalytic (C) subunit of this enzyme. On the other hand, membrane exhibited increased lipid methyltransferase activity after preincubation with MgATP and C subunit. Prephosphorylation of membranes stimulated the total [3H]-methyl incorporation into SL lipids assayed at 0.15 µM [3H]AdoMet due to an enhancement of Vmax and without changes in the Km value for AdoMet. Analysis of the methylated lipid products revealed an increased methyl group incorporation into a nonpolar lipid fraction whereas phosphatidylethanolamine-N-methylation was not affected by phosphorylation. The results suggest that the cyclic AMP-mediated signal transduction at the level of cardiac SL is not affected by methylation-induced modifications of the membrane lipid microdomains. On the other hand, an intrinsic SL lipid methyltransferase activity is apparently not related to the N-methylation of phospholipids, is modulated by cyclic AMP-dependent protein phosphorylation.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1432-1955
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Infective hookworm larvae ofAncylostoma caninum showed chemotaxis on agar plates in a dog serum gradient. This chemotactic behaviour remain unaltered using an ultrafiltrated serum fraction with a molecular weight less than 500. Gelfiltration of this ultrafiltrated fraction revealed a factor with a molecular weight of 480 causing chemotaxis. The chemotactic activity of the factor was destroyed after a pronase treatment. We conclude that the factor could be a polypeptide.
    Type of Medium: Electronic Resource
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