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  • 1
    ISSN: 1432-1939
    Keywords: Submerged macrophytes ; Annuals ; Seed size ; Seed bank ; Temporary Mediterranean marsh
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The abundance and composition of the submerged macrophyte seed bank in the Doñana marsh (southwestern Spain) was evaluated to assess its relationship with the overlying vegetation. The results obtained demonstrate the existence of a dense seed-bank, both in terms of the number of seeds and their biomass, which represented about 10% (5% for angiosperms and 〉20% for Charophyta) of the total plant biomass, which ensures the maintenance of the annual submerged macrophyte populations of the seasonally inundated Donñana marsh. Seed bank and established vegetation were coupled, as reflected in the existence of significant correlations between their structure and abundance. This coupling was lacking for Charophyta, whose oospores are widespread and abundant across the marsh, even at locations where they are absent, or rare, in the established vegetation. These differences between the seed bank of annual angiosperms and Charophyta appear to reflect, in part, structural differences between angiosperm seeds and Charophyta oospores, with important ecological consequences. An important aspect of these differences is the allocation of Charophyta reproductive effort to many small propagules lacking embryo storage, compared to those of angiosperms, which ensures their efficient dispersal and numerical abundance in the seed bank.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Pflügers Archiv 437 (1999), S. 517-522 
    ISSN: 1432-2013
    Keywords: Key words Electronic autoradiography ; Enzyme heterogeneity ; α Isoforms ; Isoform-specific antibodies ; Na+/K+-ATPase ; [3H]Ouabain binding ; Shark rectal gland ; Squalus acanthias
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  Purified Na+/K+-ATPase (EC 3.6.1.37) isolated from the rectal gland of Squalus acanthias was characterized in ouabain-binding studies and with respect to isoform(s) of the α peptide. To avoid enzyme inactivation [3H]ouabain equilibrium binding was carried out at 20°C. The heterogeneity of Na+/K+-ATPase isolated from shark rectal gland was similar in [3H]ouabain binding as previously seen in hydrolytic studies. The binding isotherms were compatible with the existence of a high-affinity (K dis 0.69 nM) and a low-affinity (K dis 42 nM) component of 1.46 and 0.79 nmol.(mg protein)–1, respectively. In Western blots the α peptide of the enzyme hybridized with an isoform-specific polyclonal antibody raised to an α3-specific region of the large intracellular domain of rat Na+/K+-ATPase, but not with the supposed α3-specific monoclonal antibody MA3-915 with its epitope near the N-terminus. Semi-quantitative analysis of the reaction of the α3-specific polyclonal antibody with the α peptide from the shark enzyme compared to the reaction with α peptide from rat brain enzyme indicated that this region is not exactly the same in the two species. The α peptide of shark enzyme was not recognized by α1- or α2-specific polyclonal antibodies, or by the α1-specific monoclonal antibodies 3B and F6. The large intracellular domain of Na+/K+-ATPase from shark rectal gland thus seems to be α3-like and no α isoform heterogeneity seems able to account for the heterogeneity seen in ouabain binding.
    Type of Medium: Electronic Resource
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