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  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Ultrasonics 29 (1991), S. 53-57 
    ISSN: 0041-624X
    Keywords: attenuation ; impedance ; instrument ; liquids ; velocity
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Ultrasonics 30 (1992), S. 403-405 
    ISSN: 0041-624X
    Keywords: attenuation ; impedance ; liquids ; ultrasonic velocity
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Ultrasonics 29 (1991), S. 58-62 
    ISSN: 0041-624X
    Keywords: attenuation ; impedance ; instrument ; liquids ; velocity
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Planta 186 (1992), S. 282-293 
    ISSN: 1432-2048
    Keywords: Guard cell ; Patch clamp ; Plasma membrane ; Potassium channels ; Zea (K+ currents)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Knowledge of ion fluxes in the dumbell-shaped guard cells of grass species has been limited by the difficulty of obtaining isolated epidermes or guard-cell protoplasts for use in radioactive-tracer or electrophysiological studies. We describe here a method for isolating guard-cell protoplasts from Zea mays L. Whole-cell patch clamp has been used to measure K+-channel current across the plasma membrane surrounding these protoplasts. Two populations of K+-permeable channels have been identified. Hyperpolarization of the membrane to potentials (Vm) more negative than -100 mV results in inward K+ current through one population of channels. Inward current activation is faster than in the dicotyledon, Vicia faba L. (mean activation half-time 26 ms (Z. mays) versus 123 ms (V. faba) at Vm=-180 mV). Steady-state current density is less than in V. faba (-22 μA · cm−2 (Z. mays) versus -40 μA · cm−2 (V. faba) at Vm=- 180 mV in 12 mM external K+). Depolarization of the membrane to potentials more positive than -20 mV results in outward K+ current through a second population of channels; these channels activate and (upon repolarization of the membrane) deactivate more slowly than in V. faba (mean activation half-time 375 ms (Z. mays) versus 187 ms (V. faba) at Vm=+ 80 mV) but result in a similar steady-state current density (23.8 μA · cm−2 (Z. mays) versus 28.7 μA · cm−2 (V. faba) at Vm= + 80 mV with 105 mM internal K+). Omission of K+ eliminates the current. The K+ current is sensitive to both internal and external Ca2+ concentration: increasing internal Ca2+ from 2 nM to 0.2 μM or increasing external Ca2+ from 1 mM to 8.5 mM reduces the magnitude of both inward and outward current.
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  • 5
    ISSN: 1432-2048
    Keywords: Guard cell ; Patch clamp ; Potassium channel (kinetics) ; Stomate ; Vicia ; Zea
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We describe and compare inward and outward whole-cell K+ currents across the plasma membrane surrounding guard-cell protoplasts from the dicotyledon, Vicia faba, and the graminaceous monocotyledon, Zea mays. Macrosopic whole-cell current is considered in terms of microscopic single-channel activity, which involves discrete steps between conducting (open) and nonconducting (closed) states of the channel protein. Kinetic equations are used to model the number of open and closed states for channels conducting K+ influx (K(in)) and K+ efflux (K(out)) in the two species, and to calculate the rate at which open-closed transitions occur. The opening and closure of K(in) channels in both Vicia and Zea follow single-exponential timecourses, indicating that K(in)-channel proteins in each species simply fluctuate between one open and one closed state. In both species, opening of K(in) channels is voltage-independent, but closure of K(in) channels is faster at more positive membrane potentials. In response to identical voltage stimuli, K(in) channels in Zea open and close approximately three times as fast as in Vicia. In contrast to K(in), K(out) channels in Zea open and close more slowly than in Vicia. The closure of K(out) channels follows a single-exponential timecourse in each species, indicating one open state. The kinetics of K(out)-channel opening are more complicated and indicate the presence of at least two (Vicia) or three (Zea) closed states.
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