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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 98 (1987), S. 191-196 
    ISSN: 1432-1424
    Keywords: amine ; porter ; Chara australis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The rate of transport of amine ions intoChara australis internodes is studied by measuring changes in membrane current when amine solutions are presented to voltage-clamped cells. The dependence of this rate on ion concentration is investigated for a series of alkyl-amine ions: methyl-, ethyl-, isopropyl-, dimethyl-, trimethyl- and tetramethylammonium. A Michaelis-Menten relationship is displayed by all except tri- and tetramethylammonium, where currents are irregular and difficult to reproduce. Evidence suggests that the different ions cross the plasmalemma via a common uniport.K M values for this porter increase as the amine ion becomes more highly substituted. TheV m values are similar for all amines and lie within the range 10 to 100 mA m−2 (for cell potential at −200 mV). The changes inK M indicate that hydrogen bonding may be involved in the binding interaction.V m varies with external pH in a way which suggests that an ionizable group on the transport protein with pKa≈5.8 directly affects the transport rate.K M is independent of external pH over the range 4.5 to 10.5
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 108 (1989), S. 153-164 
    ISSN: 1432-1424
    Keywords: K+ channel ; permeation kinetics ; patch clamp ; Chara australis ; cytoplasmic drop ; diffusion limited
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary We report a study of a potassium-selective channel in the membrane delineating cytoplasmic drops fromChara australis. The relatively large conductance (170 pS in 150 mol/m3 (mm) KCl), high ion selectivity (P Cl/P K=0.015±0.01) and voltagedependent kinetics of this channel indicate that it is a type of maxi-K channel commonly found in animal cells but not previously detected in any plant cell. The current-voltage (I/V) characteristic of these channels was examined in drop-attached and in excised outside-out patches using the patch-clamp technique, over the unusually large voltage range of −250 to 200 mV. TheI/V characteristic is nonlinear and shows saturation at extreme voltages; the current also saturates at high [K+]. In solutions with symmetrical KCl concentrations the saturation behavior of the current is asymmetrical. The permeability of the channel depends on whether it is observed in excised or in drop-attached membrane patches. Here we investigate the main factors affecting the permeation of K+ ions through this maxi-K channel. We present the first direct evidence for the importance of diffusion external to the pore in limiting ion flow through maxi-K channels. The data are consistent with an ion translocation mechanism whose current is limited (i) at high voltages by ion diffusion external to the pore and (ii) at high [K+] by the maximum transport rate of the channel. We fit the data to a diffusion-limited pore model in which the pore exhibits saturation described by Michaelis-Menten kinetics with aK m=50±25 mol/m3 andG max=300±20 pS.
    Type of Medium: Electronic Resource
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