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  • 1
    Publication Date: 2019-07-16
    Repository Name: EPIC Alfred Wegener Institut
    Type: Article , isiRev
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  • 2
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 353 (1991), S. 758-762 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] To investigate the primary steps in hormone action we have studied the effect of auxins in the intact epidermis, whole cells and cell-free membrane patches. Anion channels were characterized by their responses to phytohormones and capability to depolarize the membrane potential. When epidermal ...
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  • 3
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 344 (1990), S. 593-594 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] SIRWe wish to draw attention to the significance of the recent report1 that inositol 1,4,5-trisphosphate (InsP3) opens Ca2+ channels in the vacuolar membrane (tonoplast) of higher plants. This finding has broad implications for the regulation of ion transport at this membrane during signal ...
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  • 4
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Previously we assigned the mouse nude locus to a region of less than 1 Mb within a yeast artificial chromosome (YAC) contig on mouse chromosome 11 (ref. 5). The derivation of a new microsatellite marker, DD244, allowed us to place the nude locus into an interval covered by only three YAC clones, ...
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Planta 188 (1992), S. 206-214 
    ISSN: 1432-2048
    Keywords: Auxin ; Guard cell ; H+-ATPase ; Plasma membrane ; Proton current (voltage-dependence) ; Vicia (H+-ATPase)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Stomatal movement is controlled by external and internal signals such as light, phytohormones or cytoplasmic Ca2+. Using Vicia faba L., we have studied the dose-dependent effect of auxins on the modulation of stomatal opening, mediated through the activity of the plasma-membrane H+-ATPase. The patch-clamp technique was used to elucidate the electrical properties of the H+-ATPase as effected by growth regulators and seasonal changes. The solute composition of cytoplasmic and extracellular media was selected to record pump currents directly with high resolution. Proton currents through the ATPase were characterized by a voltage-dependent increase in amplitude, positive to the resting potential, reaching a plateau at more depolarized values. Upon changes in extracellular pH, the resting potential of the cell shifted with a non-Nernst potential response (±21 mV), indicating the contribution of a depolarizing ionic conductance other than protons to the permeability of the plasma membrane. The use of selective inhibitors enabled us to identify the currents superimposing the H+-pump as carried by Ca2+. Auxinstimulation of this electroenzyme resulted in a rise in the outwardly directed H+ current and membrane hyperpolarization, indicating that modulation of the ATPase by the hormone may precede salt accumulation as well as volume and turgor increase. Annual cycles in pump activity (1.5–3.8 μA · cm-2) were expressed by a minimum in pump current during January and February. Resting potentials of up to -260 mV and plasmamembrane surface area, on the other hand, did not exhibit seasonal changes. The pump activity per unit surface area was approximately 2- to 3-fold higher in guard cells than in mesophyll cells and thus correlates with their physiological demands.
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    European biophysics journal 21 (1993), S. 403-408 
    ISSN: 1432-1017
    Keywords: Anion channel ; Guard cell ; Stilbene derivatives ; Voltage dependence ; Gating ; Kinetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract An anion channel in the plasma membrane of guard cells (GCAC1) provides a regulatory element for the voltage-dependent release of anions during stomatal closure (Keller et al. 1989) as well as excitability (Hedrich et al. 1990). Recognition sites for plant growth hormones on the extracellular surface of GCAC1 further indicate that this channel may also serve as a transduction element in hormone signaling (Marten et al. 1991 a). Stilbene derivatives were used to study the inhibitor-structure channel-function relationship of GCAC1. We have analyzed the activity, voltage-gate and kinetics of this channel as affected by stilbenes. The stilbene derivatives SITS and DNDS caused a shift in activation potential and a decrease in the peak current amplitude. Channel block through the action of DIDS, on the other hand, was not accompanied by a shift in voltage-dependence. Differences in the dose-dependence of the two effects give clues to the presence of channel sites responsible for gate-shifting and block. The ability to inhibit anion currents (Kd) increased in the sequence: SITS (4 µM) 〈 DNDS (0.5 µM) 〈 DIDS (0.2 µM). All inhibitors reversibly blocked the anion channel from the extracellular side. Channel block on the level of single anion-channels is characterized by a reduction of long open-transitions into flickering bursts and a decrease in channel amplitude.
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    European biophysics journal 22 (1994), S. 399-403 
    ISSN: 1432-1017
    Keywords: Electrogenic pumps ; Vacuolar-type ; Voltage-dependence ; Temperature-dependence ; Reversion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract The vacuolar H+-ATPase is essential for the creation and maintenance of solute gradients. Knowledge of the reversal potential, expressed by the voltage and pH dependence of the pump may allow to determine the activity range of the enzyme. In the whole-vacuole configuration of the patch-clamp technique the application of Mg-ATP elicited inward-directed currents through the H+-ATPase. Reversal of the pump current was obtained in the presence of a pH gradient across the membrane (inside acid) by replacement of Mg-ATP by Mg-ADP and Pi. The active nature of this nucleotide-dependent transport process is reflected by a Q10 of 3.2. The voltage-dependence of the pump was elucidated by voltage-steps to various depolarizing and hyperpolarizing potentials. In the presence of Mg-ATP the current-voltage relationship of the pump current is characterized by an almost linear increase of the steady state current between 20 mV and 100 mV, tending to saturate at more positive potentials. The voltage-dependence of the inward pump current could be described by a pseudo-two-state model.
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Immunogenetics 38 (1993), S. 381-381 
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1573-4927
    Keywords: esterase-18 ; rat genetics ; liver specific ; linkage group V ; cluster 2
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A new liver-specific rat carboxylesterase isozyme (EC 3.1.1.1) designated esterase-18 (ES-18) is described. Genetic variation of ES-18 was examined in 93 inbred strains and substrains and a structural locusEs-18 was suggested, coding for either the presence (Es-18 a) or the absence (Es-18 b) of the isozyme. Linkage studies involving two backcross series revealed thatEs-18 resides in cluster 2 of LGV. No recombination betweenEs-18 and other cluster 2 loci was found in 19 lines of two RI strain sets or in the backcross series.
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Plant molecular biology 26 (1994), S. 1637-1650 
    ISSN: 1573-5028
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
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