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  • Tobacco BY-2 cells  (2)
  • ^2^7Al NMR  (2)
  • 1
    Digitale Medien
    Digitale Medien
    Amsterdam : Elsevier
    Phytochemistry 32 (1993), S. 771-775 
    ISSN: 0031-9422
    Schlagwort(e): Camellia sinensis ; Theaceae ; ^1^9F NMR ; ^2^7Al NMR ; aluminium complexes ; catechin ; fluorine ; kinetics.
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie , Chemie und Pharmazie
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Amsterdam : Elsevier
    Phytochemistry 31 (1992), S. 1215-1218 
    ISSN: 0031-9422
    Schlagwort(e): Camellia sinensis ; Camelliaceae ; ^2^7Al NMR ; aluminium complex ; catechin ; fluorine ; leaf ; organic acid ; phenolic acid
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie , Chemie und Pharmazie
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 3
    ISSN: 1615-6102
    Schlagwort(e): Cell cycle ; Microtubule ; Microtubule organizing center ; Synchronization ; Tobacco BY-2 cells
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary A 49 kDa protein in tobacco BY-2 cells has been found to be cross-reactive with antibodies raised against a 51 kDa protein that was isolated from sea urchin centrosomes and identified as a microtubule-organizing center (MTOC) in animal cells. Tracing the fate of the 49 kDa protein during progression of the cell cycle in highly synchronized tobacco BY-2 cells revealed that this protein was colocalized with plant microtubules (MTs): the location of the 49 kDa protein coincided with preprophase bands (PPBs), mitotic spindles and phragmoplasts. Furthermore, between the M and G1 phases, the 49 kDa protein was observed in the perinuclear regions, in which the initials of MTs are organizing to form cortical MTs. At the G1 phase the location of the 49 kDa protein in the cell cortex coincided with that of the cortical MTs. It appeared that the 49 kDa protein in the cell cortex was transported as granules from the perinuclear regions. Thus, it is highly probable that the 49 kDa protein, which reacts with antibodies against the 51 kDa protein in sea urchin centrosomes, plays the role of an MTOC in plant cells. Thus, the mechanisms for organizing MTs in higher organisms appear to share a common protein, even though the organization of MTs is superficially very different in plant and animal cells.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 4
    Digitale Medien
    Digitale Medien
    Springer
    Protoplasma 198 (1997), S. 202-209 
    ISSN: 1615-6102
    Schlagwort(e): Cell cycle ; Elongation factor 1α ; Microtubule reorganization ; Microfilament ; Tobacco BY-2 cells
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary The sites of microtubule (MT) reorganization were examined in synchronized tobacco BY-2 cells. The MTs of these cells were completely destroyed by a combined cold and drug treatment at 0 °C with 100 μM propyzamide for 3 h. After the cells were washed and cultured at 30 °C, the reorganization of MTs was observed in detail. Sites for MT reorganization at each stage of the cell cycle were identified on the cell cortex and nuclei, the mitotic apparatus, the nuclei (or the nuclei and cell cortex), and the cell cortex in the S-G2 phase, M phase, M/G1 interface, and g1 phase, respectively. The polypeptide synthesis elongation factor (EF)-1α is co-localized with these sites of MT reorganization. At some stages, microfilaments (MFs) were found to be involved in the reorganization of MTs. Based on these results, the mode of MT reorganization during cell cycle progression is discussed.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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