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  • 1
    ISSN: 0886-1544
    Keywords: intermediate filaments ; microtubules ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Sea urchin spermatozoa, eggs, and embryos were labeled with the universal antibody against the intermediate filament proteins (anti-IFA) described by Pruss et al. [Cell 27:419-428, 1981] and with anti-beta-tubulin. Localization of these antibodies was by indirect immunofluorescence microscopy. Cytoskeleton of unfertilized eggs, prepared according to a procedure adapted from Kane [Exp. Cell Res. 162:495-506, 1986] or as described by Dufresne et al. [Biochem. Cell Biol. 66:780-791, 1988], and reacted with the anti-IFA demonstrate a uniformly stained background except for the nuclear areas, which appear as dark rings. During the first cell cycle, the anti-IFA staining pattern coincides with that of spindle-associated tubulin but not with the cortical pattern of microtubules. Swimming embryos reacted with the anti-IFA show a labeling located on the cilia and within the cytoplasm of each individual cell of the larva. In spermatozoa, the labeling occurs all along the flagellae. Immunoblots of proteins from eggs and embryos reveal one major protein of 117 kDa and sometimes a component of 66 kDa, both of which cosediment with tubulin during the isolation procedure of microtubules described by Vallee and Bloom [Proc. Natl. Acad. Sci. USA 80:6259-6263, 1983]. These data show that proteins homologous to the intermediate filament proteins reported in vertebrate cells are present in both gametes of sea urchins. The specific localization ofthese proteins in the spindle, the flagella, and the cilia suggest that they may play a significant role in the organization and function of the microtubular lattice of the spermatozoa and of the embryo.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0886-1544
    Keywords: intermediate filaments ; phosphorylation ; sea urchin embryos ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The effects of 6-dimethylaminopurine (6-DMAP) on the length of the cell cycle and on the state of phosphorylation of a putative intermediate filament protein, p117, have been studied in sea urchin embryos. Embryos were transferred into sea water containing 600 μM 6-DMAP at 0.5, 2 or 5 min after insemination, and incubated for 30 or 90 min. The effects of 6-DMAP on cell cycle length were studied by determining the time required for completion of mitosis upon return of the embryos in normal sea water. In all instances, except for the embryos transferred 0.5 min after insemination (AI) and incubated for 30 min, the duration of the M phase was shortened compared to controls, being faster in the embryos incubated for 90 minutes compared to the 30 min incubation period. However, embryos transferred 0.5 min AI have a longer M-phase than those transferred 2 minutes or later after fertilization, suggesting that between 0.5 and 2 min after fertilization, critical phosphorylating events occur which affect the commitment of the cells to enter M-phase.To study the pattern of p117 phosphorylation during the cell cycle, the eggs were transferred 2 minutes after fertilization in presence of 600 μM 6-DMAP and with 200 μCi/ml of 32P-orthophosphate. Analyses of 32P-labelled proteins after exposure of SDS-PAGE gels and their corresponding blots suggested that phosphorylation of p117 greatly increases at the time of pronuclear fusion, and then declines slightly at prophase-metaphase. This decrease is markedly enhanced when the cells are treated with 6-DMAP during metaphase in order to induce a premature breakdown of the mitotic apparatus. A causal link is suggested between the level of phosphorylation of p117 and its state of assembly. © 1994 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
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  • 3
    ISSN: 1572-879X
    Keywords: ethylene aromatization ; ZSM-5 zeolite ; Zn oxide based co-catalysts ; hybrid catalysts ; hydrogen spillover
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The involvement of hydrogen back-spillover is confirmed for the aromatization of ethylene. Using hydrogen monitoring during catalytic reactions with ethylene, it has been observed that the amount of hydrogen in the gaseous effluents is much more important on hybrid catalysts than on pure ZSM-5 zeolites. The active sites on ZnO based co-catalysts are believed to be partial reduction zinc sites created during the induction period. ZnO precipitate favors the release of hydrogen species as ethane. ZnO/Al2O3 co-precipitate favors hydrogen recombination.
    Type of Medium: Electronic Resource
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