ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Macromolecules 6 (1973), S. 456-459 
    ISSN: 1520-5835
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Macromolecules 16 (1983), S. 1212-1215 
    ISSN: 1520-5835
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 3
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 69 (1982), S. 35-40 
    ISSN: 1432-1424
    Keywords: axon ; hydrostatic pressure ; K currents ; kinetics ; activation volume
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The effect of pressure upon the delayed, K, voltage-clamp currents of giant axons from the squidLoligo vulgaris was studied in axons treated with 300nm TTX to block the early, Na, currents. The effect of TTX remained unaltered by pressure. The major change produced by pressures up to 62 MPa is a slowing down of the rising phase of the K currents by a time scaling factor which depends on pressure according to an apparent activation volume, ΔV∓, of 31 cm3/mole at 15°C; ΔV∓ increased to about 42 cm3/mole at 5°C. Pressure slightly increased the magnitude, but did not produce any obvious major change in the voltage dependence, of the steady-state K conductance estimated from the current jump at the end of step depolarizations of small amplitude (to membrane potentials,E, ≦20 mV) and relatively short duration. At higher depolarizations, pressure produced a more substantial increase of the late membrane conductance, associated with an apparent enhancement of a slow component of the K conductance which could not be described within the framework of the Hodgkin-Huxley (HH)n 4 kinetic scheme. The apparent ΔV∓ values that characterize the pressure dependence of the early component of the K conductance are very close to those that describe the effect of pressure on Na activation kinetics, and it is conceivable that they are related to activation volumes involved in the isomerization of the normal K channels. The enhancement of the slow component of membrane conductance by pressure implies either a large increase in the conductance of the ionic channels that are responsible for it or a strong relative hastening of their turn-on kinetics.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 4
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 69 (1982), S. 23-34 
    ISSN: 1432-1424
    Keywords: axon ; hydrostatic pressure ; Na currents ; kinetics ; temperature ; activation volume
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The effects of hydrostatic pressures up to 62 MPa upon the voltage-clamp currents of intact squid giant axons were measured using mineral oil as the pressure transmitting medium. The membrane resistance and capacitance were not appreciably affected over the whole range of pressures explored. The predominant effect of pressure is to slow the overall kinetics of the voltage-clamp currents. Both the early (Na) currents and the delayed (K) ones were slowed down by approximately the same time scale factor, which was in the range of 2 to 3 when pressure was increased from atmospheric to 62 MPa. Finer details of the effects, most evident at moderate depolarizations, are: the apparent initial delay in the turn-on of Na currents is increased by pressureless than is the phase of steepest time variation, and the later decay is slowedmore than is the rising phase. The initial time course of the currents at high pressures can be made to overlap with that at normal pressure by a constant time compression factor, Θm, together with a small, voltage-dependent delay. In a given axon, Θm was fairly independent of voltage, and it increased exponentially with pressure according to an apparent activation volume, ΔV∓, ranging between 32 and 40 cm3/mole. ΔV∓ tended to decrease with increasing temperature. Contrary to what is observed for moderate or large depolarizations, the kinetics of Na inactivation produced by conditioning prepulses of −50 or −60 mV was little affected over the whole range of pressures explored. Inferences about the pressure dependence of the steady-state Na activation were made from the comparison of the plots of early peak currents,I p, versus membrane potential,E. The Na reversal potential,E Na, and the slope of the plots nearE Na did not change significantly with pressure, but the peak Na conductancevs. E relationship was shifted by about +9 mV upon increasing pressure to 62 MPa. Steady-state Na inactivation,h ∞, was slightly affected by pressure. At 62 MPa the midpoint potential of theh ∞ (E) curve,E h, was shifted negatively by about 4 mV, while the slope atE h decreased by about 38%. Under the tentative assumption that pressure directly affects the gating of Na channels, the Na activation data follows a simple Hodgkin-Huxley scheme if the opening of anm gate involves an activation volume of about 58 Å3 and a net volume increase of about 26 Å3. However, a self-consistent description of the totality of the effects of pressure on Na inactivation cannot be obtained within a similar simple context.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 5
    Electronic Resource
    Electronic Resource
    Springer
    European biophysics journal 1 (1975), S. 221-237 
    ISSN: 1432-1017
    Keywords: Fluorescence Polarization ; Nerve
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract The polarized components of the extrinsic fluorescence of squid giant axons stained with 2,6-MANS or 1,8-MANS were studied. The polarization properties of the fluorescence changes associated with voltage-clamp pulses were found to be very different from those of the static fluorescence, supporting the notion that the optical changes involve highly oriented membrane adsorbed fluorophores. The theoretical expectations according to this hypothesis are discussed in detail. The experimental results are in good agreement with the theory assuming that possible probes reorientations are solely due to the action of the applied electric field upon the probes electric dipole. The quantitative analysis of the data for 2,6 MANS provides a fairly accurate determination of the orientation of the membrane bound 2,6-MANS molecules responsible for the fluorescence changes. Such orientation appears to be independent of the membrane face exposed to staining. The data for 1,8-MANS indicate a very different orientation of this isomer. The results suggest a profitable use of extrinsic fluorophores for studies of the structural organization of nerve membranes.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 6
    Electronic Resource
    Electronic Resource
    Springer
    European biophysics journal 1 (1974), S. 27-45 
    ISSN: 1432-1017
    Keywords: Fluorescence ; Nerves ; Bilayers
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract Changes in extrinsic fluorescence intensity, associated with step changes in membrane potential, have been studied in intracellularly or extracellularly stained squid axons, and in lipid bilayers, using six different aminonaphthalene dyes: 1,8-TNS; 2,6-TNS; 1,8-MANS; 2,6-MANS; 2,6-ANS and NPN. In all preparations the optical signals were found to be roughly proportional to the voltage applied. All signals had a very fast initial component, which was followed in some case by a slower change in the same direction. The slow component was observed only in intracellularly stained axons, and not for all chromophores studied. 1,8-TNS, 1,8-MANS and 2,6-MANS yielded the largest fluorescence signals in all preparations. The sign of these signals was independent of the type of membrane studied. However, the fluorescence changes of 2,6-MANS were opposite to those of 1,8-TNS and 1,8 MANS. Staining of both sides of the axolemma with 1,8-MANS or 2,6-MANS showed that these dyes yield larger signals when applied to the extracellular face. The changes in fluorescence light intensity of 2,6-TNS, 2,6-ANS and NPN were smaller and their sign depended on the membrane preparation studied. The comparison of the extrinsic fluorescence signals from the nerve membrane and the phosphatidylcholine bilayer suggests strong similarities between the basic structures of the two systems. The variety of observed signals cannot be easily interpreted in terms of changes in membrane structure. A possible alternative interpretation in terms of electrically induced displacements, rotations and changes in partition coefficient of bound chromophores, is discussed.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 7
    Electronic Resource
    Electronic Resource
    Springer
    European biophysics journal 17 (1989), S. 53-59 
    ISSN: 1432-1017
    Keywords: Sodium channel ; gating current ; fluctuation analysis ; patch clamp
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract Asymmetric displacement currents, I g , associated with the gating of nerve sodium channels have been recorded in cell-attached macropatches of Xenopus laevis oocytes injected with exogenous mRNA coding for rat-brain-II sodium channels. The I g properties were found to be similar to those of gating currents previously observed in native nerve preparations. I g fluctuations were measured in order to ascertain the discreteness of the conformational changes which precede the channel opening. The autocorrelation of the fluctuations is consistent with a shot-like character of the elementary I g contributions. The variance of the fluctuations indicates that most of the gating-charge movement that accompanies the activation of a single sodium channel occurs in 2 to 3 brief packets, each carrying an equivalent of about 2.3 electron charges.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 8
    Electronic Resource
    Electronic Resource
    Springer
    European biophysics journal 18 (1990), S. 25-32 
    ISSN: 1432-1017
    Keywords: Sodium channel ; Gating currents ; Mammalian cells ; Patch clamp
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract Ionic and gating currents from voltage-gated sodium channels were recorded in mouse neuroblastoma cells using the path-clamp technique. Displacement currents were measured from whole-cell recordings. The gating charge displaced during step depolarizations increased with the applied membrane potential and reached saturating levels above 20 mV Prolonged large depolarizations produced partial immobilization of the gating charge, and only about one third of the displaced charge was quickly reversed upon return to negative holding potentials. The activation and inactivation properties of macroscopic sodium currents were characterized by voltage-clamp analysis of large outside-out patches and the single-channel conductance was estimated from nonstationary noise analysis. The general properties of the sodium channels in mouse neuroblastoma cells are very similar to those previously reported for various preparations of invertebrate and vertebrate nerve cells.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 9
    Electronic Resource
    Electronic Resource
    Springer
    European biophysics journal 16 (1988), S. 73-81 
    ISSN: 1432-1017
    Keywords: UV damage ; sodium channels ; axon ; UV absorption ; polarization ; tryptophan
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract UV irradiation of squid giant azons at wavelengths of 280 or 290 nm produces nearly the same rate of irreversible decrease of sodium currents. The rate of photodeactivation is unaffected by extensive removal of axoplasm with pronase, and it is independent of temperature in the range 5° to 20°C. The photochemical effect appears to be all or nothing. It does not alter the time course and the voltage dependence for activation and inactivation of the residual currents. Similar deactivation rates were produced by irradiations of the same intensity, but linearly polarized either parallel or perpendicular to the axon. The efficiency of the deactivation process is close to that expected if it was caused by the photooxidation of a single tryptophan residue per sodium channel. Owing to the geometry of the preparation the lack of polarization asymmetry suggests that this residue assumes nearly random (or pseudo-random) orientation in the three-dimensional structure of the sodium channel corresponding to the closed state.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 10
    ISSN: 1432-1017
    Keywords: Potassium channel ; KAT1 ; Voltage dependence ; Cesium block ; pH dependence ; Kinetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract We have investigated the electrophysiological basis of potassium inward rectification of the KAT1 gene product from Arabidopsis thaliana expressed in Xenopus oocytes and of functionally related K+ channels in the plasma membrane of guard and root cells from Vicia faba and Zea mays. The whole-cell currents passed by these channels activate, following steps to membrane potentials more negative than −100 mV, with half activation times of tens of milliseconds. This voltage dependence was unaffected by the removal of cytoplasmic magnesium. Consequently, unlike inward rectifier channels of animals, inward rectification of plant potassium channels is an intrinsic property of the channel protein itself. We also found that the activation kinetics of KAT1 were modulated by external pH. Decreasing the pH in the range 8.5 to 4.5 hastened activation and shifted the steady state activation curve by 19 mV per pH unit. This indicates that the activity of these K+ channels and the activity of the plasma membrane H+-ATPase may not only be coordinated by membrane potential but also by pH. The instantaneous current-voltage relationship, on the other hand, did not depend on pH, indicating that H+ do not block the channel. In addition to sensitivity towards protons, the channels showed a high affinity voltage dependent block in the presence of cesium, but were less sensitive to barium. Recordings from membrane patches of KAT1 injected oocytes in symmetric, Mg2+-free, 100 mM-K+, solutions allowed measurements of the current-voltage relation of single open KAT1 channels with a unitary conductance of 5 pS. We conclude that the inward rectification of the currents mediated by the KAT1 gene product, or the related endogenous channels of plant cells, results from voltage-modulated structural changes within the channel proteins. The voltage-sensing or the gating-structures appear to interact with a titratable acidic residue exposed to the extracellular medium.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...