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  • 1990-1994  (2)
  • Ion channel blockade  (1)
  • Mesophyll (cells, protoplasts)  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Changes in the density of microtubular networks in mesophyll cells and mesophyll derived protoplasts of Nicotiana and Triticum during leaf development (1993)
    Springer
    Planta 190 (1993), S. 10-16 
    Details
    ISSN: 1432-2048
    Keywords: Leaf development ; Mesophyll (cells, protoplasts) ; Microtubule (patterns, density) ; Nicotiana ; Tissue culture (in vitro competence) ; Triticum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Changes in the density of microtubular mesh-works were analysed in mesophyll cells and mesophyll derived protoplasts of Nicotiana tabacum L. and Triticum aestivum L. during leaf development. The main purpose of this study was to test whether the low density, if not lack, of microtubular networks recently described in protoplasts that had been isolated from fully differentiated mesophyll cells happened during protoplast isolation or whether the loss of microtubules actually occurred during differentiation of the leaf tissue. Immunofluorescence microscopy showed that the density of the microtubular cytoskeleton in the leaf tissue decreased steadily after cessation of cell growth in both species. Nevertheless, in Triticum microtubule disappearance was swifter and occurred along a gradient from the base to tip of the leaf, a phenomenon reflecting the differences in the ontogeny between the dicotyledonous Nicotiana and the mono-cotyledonous Triticum leaves. Protein extraction from leaf tissues and Western blot analysis indicated that in both species the disappearance of microtubules was the result of a degradation of tubulin and not only due to a depolymerisation into tubulin subunits. When the cell walls were removed from live cells and the protoplasts released, the original patterns of the microtubules became obscured and, particularly in differentiated cells, the integrity and density of the microtubule strands deteriorated. The potential application of the density of the microtubular cytoskeleton as a marker in studies on differentiation and dedifferentiation in mesophyll cells and protoplasts is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00195669
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  • 2
    Electronic Resource
    Electronic Resource
    Effects of polycations on ion channels formed by neutral and negatively charged alamethicins (1994)
    Springer
    European biophysics journal 23 (1994), S. 155-165 
    Details
    ISSN: 1432-1017
    Keywords: Alamethicin ; Ion channel blockade ; Planar lipid bilayers ; Polycations
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract The effects of the peptide polycations salmon protamine (M r = 4332,z = + 21) and poly-l-lysine (M r ≅ 100,00,z ≅ + 775) on ion channels formed by synthetic alamethicin Alm-F30 (one negative charge), natural Alm-F50 (neutral) and phosphorylated Alm-F50 (two negative charges) reconstituted in planar lipid bilayers have been studied at the single channel level. It was observed that both polycations in micromolar concentrations transiently block ion permeation through the channels formed by each alamethicin analogue, although in case of the neutral Alm-F50 to a significantly lesser extent. Poly-l-lysine showed to be more effective than protamine in blocking these channels. If either polycation is present in the cis-compartment, blockade occurs only at cis positive membrane voltages. At constant polycation concentration, dwell times in the blocked state increase when salt concentration is lowered, and decrease at acidic pH with an apparent pK of 4.8. Mean lifetime of blockade events shortens when membrane voltage is increased, which suggests that both polycations may permeate through the oligomeric alamethicin channels if conductance levels are 〉 2. We suggest that blockade is caused by electrostatic binding of a single polycation molecule to the C-terminal channel mouth; in case of Alm-F30, Glu18 has to be considered as the putative binding site. Our results provide further evidence for the barrel-stave model and a parallel orientation of dipole monomers in the channel aggregate, the C-termini facing the membrane side with the more positive membrane potential.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01007607
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    Paper (German National Licenses)
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