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  • Amiprophos-methyl  (1)
  • Reaction-diffusion  (1)
  • 1
    ISSN: 1615-6102
    Keywords: Amiprophos-methyl ; Microtubule organizing center
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A one hour exposure to 3 μM amiprophos-methyl (APM) depolymerizes all MT arrays in cells from higher plant suspension cultures. On removal of APM, MT repolymerization sites are detected using immunofluorescent staining. During interphase, Mt arrays return uniformly dispersed across the cell cortex with transverse arrays in elongated cells and random arrays in isodiametric cells. During cell division, MT arrays return as follows: Prophase-MT arrays return in association with the nuclear envelope. Metaphase-MTs return associated with chromosomes. Teleophase-MTs return in apparent association with the reforming nuclear envelope and as aberrant phragmoplasts. MTOCs in higher plant cells may be membrane associated at many stages in the cell cycle. Isolated, condensed chromosomes are capable of nucleating MTs, which can attain small, spindle-like configurations.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1615-6102
    Keywords: Acetabularia acetabulum ; Whorl morphogenesis ; Reaction-diffusion ; EGTA ; Calcium receptors
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The spacing between adjacent hairs in vegetative whorls ofAcetabularia acetabulum (formerlyA. mediterranea) was earlier reported as being quantitatively responsive to calcium ion concentration in the culture medium. We here report a quantitative response to the concentration of the calcium-chelator EGTA, in the opposite sense to the effect of calcium. (Increasing [Ca2+] diminishes the spacing; increasing [EGTA] increases it.) The earlier work was interpreted in terms of control of the spacing by a putative reaction-diffusion mechanism in the cell membrane, in which a receptor R was activated by calcium-binding to initiate the process. We extend this interpretation by treating CaEGTA as an uncompetitive inhibitor of the effect of calcium on R. This leads to thermodynamic constants for CaEGTA binding to the CaR complex: ΔH 298 0 =−250 ± 60 kJ/mol; ΔS 298 0 =−820 ± 200 J/mol · K. Consistency of the concentration and temperature dependences reported here with the postulated dynamic mechanism increases the probability that this mechanism is correct.
    Type of Medium: Electronic Resource
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