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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 5 (1971), S. 225-245 
    ISSN: 1432-1424
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Evidence is presented that the transport of lipid-soluble ions through bilayer membranes occurs in three distinct steps: (1) adsorption to the membranesolution interface; (2) passage over an activation barrier to the opposite interface; and (3) desorption into the aqueous solution. Support for this mechanism comes from a consideration of the potential energy of the ion, which has a minimum in the interface. The formal analysis of the model shows that the rate constants of the individual transport steps can be determined from the relaxation of the electric current after a sudden change in the voltage. Such relaxation experiments have been carried out with dipicrylamine and tetraphenylborate as permeable ions. In both cases the rate-determining step is the jump from the adsorption site into the aqueous phase. Furthermore, it has been found that with increasing ion concentration the membrane conductance goes through a maximum. In accordance with the model recently developed by L. J. Bruner, this behavior is explained by a saturation of the interface, which leads to a blocking of the conductance at high concentrations.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 63 (1981), S. 85-92 
    ISSN: 1432-1424
    Keywords: Skeletal muscle ; K channel ; inward rectifier ; fluctuation analysis ; single-channel conductance
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary K currents and K-current fluctuations were recorded in inwardly rectifying K channels of frog skeletal muscle under voltage-clamp conditions. External application of 0.2 to 10mm Cs reduces the inward mean K current but produces a distinct increase of the spectral density of K-current fluctuations. The additional fluctuations arise from the random blocking by Cs ions. From the variance of current fluctuations, the steady-state current and the probability of the open unblocked channel an effective single-channel conductanceγ * was calculated.γ * strongly depends on the external Cs concentration (7.8 pS at 0.2mm Cs, 2.1 pS at 10mm Cs). This dependence is interpreted in terms of a two-step blocking process: (1) a fast exchange of Cs ions between the external solution and a first binding site inside the channel which leads to the Cs-modulated effective single-channel conductance, and (2) a slow Cs binding to a second site deeper in the channel which produces the observed current fluctuations. With this hypothesis we obtained a real single-channel conductance of γ≈10 pS and a real density ofn≈4 inwardly rectifying channels per μm2 of muscle surface area.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 110 (1989), S. 217-226 
    ISSN: 1432-1424
    Keywords: skeletal muscle ; patch clamp ; K+ channel ; adenosine triphosphate ; n-ethylmaleimide ; sulphydryl group
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Single K+-selective channels were studied in excised inside-out membrane patches from dissociated mouse toe muscle fibers. Channels of 74 pS conductance in symmetrical 160mm KCl solutions were blocked reversibly by 10 μm internal ATP and thus identified as ATP-sensitive K+ channels. The channels were also blocked reversibly bymm concentrations of internal adenosine, adenine and thymine, but not by cytosine and uracil. The efficacy of the reversible channel blockers was higher when they were present in internal NaCl instead of KCl solutions. An irreversible inhibition of ATP-sensitive K+ channels was observed after application of several sulphydryl-modifying substances in the internal solution: 0.5mm chloramine-T, 50mm hydrogen peroxide or 2mm n-ethylmaleimide (NEM). Largeconductance Ca-activated K+ channels were not affected by these reagents. The presence of 1mm internal ATP prevents the irreversible inhibition of ATP-sensitive K+ channels by NEM. The results suggest that internal Na+ ions increase the affinity of the ATP-sensitive K+ channel to ATP and to other reversible channel blockers and that a functionally important SH-group is located at or near the ATP-binding site.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 3 (1970), S. 54-66 
    ISSN: 1432-1424
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary A mathematical treatment is given for the flux of ions of one charge sign across lipid bilayer membranes. This treatment is a generalization of a previous analysis of the membrane conductance by D. Walz, E. Bamberg and P. Läuger which was restricted to systems with negligible space charge in the membrane. The present theory includes space charge effects, and it is no longer assumed that the electric field strength in the membrane is constant. It is found that the ohmic membrane conductivity λ0 is reduced by space charges; if only ions of one charge sign are soluble in the membrane, λ0 approaches a limiting value for increasing concentration of the permeable ion in the aqueous solution. The theory also predicts the range in which the constant field approximation is valid. It is found that space charge effects become predominant when the mean concentration of the permeable ion in the membrane exceeds 5×10−5 m. The currentvoltage characteristic of the membrane remains practically linear even in the presence of a high space charge. It is therefore concluded that the experimentally observed nonlinearity is caused mainly by the distortion of the potential energy profile of an ion due to image forces.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    European biophysics journal 23 (1994), S. 231-237 
    ISSN: 1432-1017
    Keywords: Skeletal muscle ; Potassium channel ; Channel blockage ; ATP ; AMP-PNP
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract Single ATP-sensitive potassium channels (K ATP channels) were studied in inside-out membrane patches excised from mouse skeletal muscle. Channel blockage by the non-hydrolysable ATP analogue AMP-PNP was investigated in the absence or presence of 1 mM MgCl2 with K+-rich solutions bathing the internal membrane surface. Currents through single. K ATP channels were recorded at −40 and +40 mV AMP-PNP (5 to 500 μM; Li salt) reduced the open-probability po of K ATP channels and decreased the single-channel currents at high nucleotide concentrations by approximately 10%. Half maximal reduction of po at −40 mV was observed at nucleotide concentrations of 29 μM in the absence and of 39 μM in the presence of Mg2+. The steepness of the AMP-PNP concentration-response curves was strongly affected by Mg2+, the Hill coefficients of the curves were 0.6 in the absence and 1.6 in the presence of 1 mM MgCl2. The efficacies of channel blockage by AMP-PNP at −40 and +40 mV were not significantly different. The results indicate that a K ATP channel can bind more divalent Mg2+-complexes of AMP-PNP than trivalent protonated forms of the nucleotide and that channel blockage is hardly affected by the membrane electric field. To estimate the contribution of lithium ions to the observed results, we studied the effects of LiCl (0.8 to 10 mM) in the Mg2+-free solution on the single channel current i. At a Li+ concentration of 10 mM, i was hardly affected at −40 mV but reduced by a factor of 0.75 at +40 mV. The results are interpreted by a fast, voltage-dependent blockage of K ATP channels by internal Li+ ions.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    European biophysics journal 4 (1978), S. 179-199 
    ISSN: 1432-1017
    Keywords: 1/f Noise ; Biological membrane ; Synthetic membrane ; Membrane pore ; Diffusion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract The present situation of 1/f noise in the passage of ions across membranes is examined. A survey of biological and synthetic membranes is given at which a l/f frequency dependence has been observed in the spectrum of voltage or current fluctuations. Empirical relations and theories of 1/f noise in membranes are critically discussed.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    European biophysics journal 2 (1976), S. 93-94 
    ISSN: 1432-1017
    Keywords: Lipid bilayer membrane ; Uncoupler of oxidative phosphorylation ; Action potential ; Active cation pump
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract Several processes at biological membranes can be simulated by experiments with artificial lipid bilayer membranes. Three selected examples are discussed: The uncoupler induced proton permeability of lipid bilayers, the initiation of action potential like voltage responses in lipid membranes, and the reconstitution of active cation pumps across planar lipid bilayers or lipid vesicles.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    European biophysics journal 19 (1991), S. 119-123 
    ISSN: 1432-1017
    Keywords: Skeletal muscle ; Potassium channel ; Patch clamp ; ATP ; Vanadate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract The inside-out mode of the patch-clamp technique was used to study adenosine-5′-triphosphate (ATP)-sensitive K+ channels in mammalian skeletal muscle. Vanadate, applied to the cytoplasmic face of excised patches, was a potent activator of ATP-sensitive K+ channels. Divalent cations (Mg2+, Ca2+) were a prerequisite for the activating process. The maximal effect was achieved using 1 mM vanadate dissolved in Ringer, increasing the open-state probability about ninefold. The active 5 + redox form of vanadate which stimulates ATP-sensitive K+ channels is likely to be decavanadate V10O inf28 sup6− . ATP concentration-response curves have Hill coefficients near three in internal Na+-rich Ringer and between one and two in internal KCl solutions. Half maximal channel blockage was observed at ATP concentrations of 4 and 8 μM in Ringer and KCl solutions, respectively. Internal vanadate shifted the curves towards higher ATP concentrations without affecting their slopes. Thus 50% channel blockage occurred at 65 μM ATP in internal Ringer containing 0.5 mM vanadate. The results indicate that the affinity and stoichiometry of ATP binding to ATP-sensitive K+ channels are strongly modulated by internal cations and that the ATP sensitivity is weakened by vanadate.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    European biophysics journal 6 (1980), S. 137-137 
    ISSN: 1432-1017
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    European biophysics journal 6 (1980), S. 138-138 
    ISSN: 1432-1017
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Type of Medium: Electronic Resource
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