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Keywords = flux gate probe

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23 pages, 14496 KiB  
Article
Hardware Design and Implementation of a High-Precision Optically Pumped Cesium Magnetometer System Based on the Human-Occupied Vehicle Platform
by Keyu Zhou, Qimao Zhang and Qisheng Zhang
Appl. Sci. 2024, 14(15), 6778; https://doi.org/10.3390/app14156778 - 2 Aug 2024
Viewed by 902
Abstract
High-precision magnetometers play a crucial role in ocean exploration, geophysical prospecting, and military and security applications. Installing them on human-occupied vehicle (HOV) platforms can greatly enhance ocean exploration capabilities and efficiency. However, most existing magnetometers suffer from low sensitivity and excessively large size. [...] Read more.
High-precision magnetometers play a crucial role in ocean exploration, geophysical prospecting, and military and security applications. Installing them on human-occupied vehicle (HOV) platforms can greatly enhance ocean exploration capabilities and efficiency. However, most existing magnetometers suffer from low sensitivity and excessively large size. This study presents a high-sensitivity, miniaturized magnetometer based on cesium optically pumped probes. The designed magnetometer utilizes a three-probe design to eliminate the detection dead zone of the cesium optically pumped probe and enable three-dimensional magnetic detection. The proposed magnetometer uses a flux gate probe to detect the three-axis magnetic field and ensure that the probe does not enter the dead zone. The three probes can automatically switch by measuring the geomagnetic elements and real-time attitude of the HOV platform. This article primarily introduces the cesium three-probe optically pump, flux gate sensor, and automatic switching scheme design of the above-mentioned magnetometer. Moreover, it is proven through testing that the core indicators, such as the accuracy and sensitivity of the cesium three-probe optically pumped and flux gate sensor, reach international standards. Finally, the effectiveness of the automatic switching scheme proposed in this study is demonstrated through drone-mounted experiments. Full article
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Figure 1

Figure 1
<p>System block diagram.</p>
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<p>The hardware of the optically pumped probe.</p>
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<p>The cesium optically pumped probe.</p>
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<p>A three-dimensional model of the cesium atomic lamp.</p>
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<p>A physical picture of the cesium atomic lamp.</p>
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<p>A cesium absorption cell model.</p>
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<p>A schematic diagram of the signal conditioning process.</p>
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<p>A circuit diagram of the signal conditioning circuit.</p>
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<p>A schematic diagram of the temperature control unit.</p>
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<p>Design diagram of the temperature control circuit.</p>
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<p>A schematic diagram of the RF excitation circuit.</p>
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<p>The structure of the single-axis flux gate probe.</p>
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<p>A schematic diagram of the detection circuit.</p>
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<p>The dimensions of the optical probe unit (unit: mm).</p>
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<p>A three-dimensional diagram of the probe assembly.</p>
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<p>The simulation results.</p>
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<p>A control flowchart for switching between three probes.</p>
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<p>A block diagram of the triaxial flux gate acquisition board.</p>
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<p>The peripheral circuit of the Zynq XC7Z020 processor chip.</p>
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<p>A schematic diagram of the absolute accuracy, sensitivity, and dynamic range testing of the optically pumped cesium magnetometer.</p>
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<p>A photograph of the magnetic shielding cylinder.</p>
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<p>A schematic diagram of gradient tolerance testing for the optically pumped cesium magnetometer.</p>
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<p>Ultra-high-uniformity magnetic field generation system.</p>
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<p>A schematic diagram of zero-field compensation testing for the triaxial flux gate probe.</p>
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<p>A schematic diagram of triaxial flux gate probe noise testing.</p>
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<p>Platform movement trajectory.</p>
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<p>Platform movement attitude.</p>
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<p>Test curves for the automatic probe switching experiment.</p>
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14 pages, 1473 KiB  
Article
The Dragon’s Paralysing Spell: Evidence of Sodium and Calcium Ion Channel Binding Neurotoxins in Helodermatid and Varanid Lizard Venoms
by James S. Dobson, Richard J. Harris, Christina N. Zdenek, Tam Huynh, Wayne C. Hodgson, Frank Bosmans, Rudy Fourmy, Aude Violette and Bryan G. Fry
Toxins 2021, 13(8), 549; https://doi.org/10.3390/toxins13080549 - 6 Aug 2021
Cited by 8 | Viewed by 6093
Abstract
Bites from helodermatid lizards can cause pain, paresthesia, paralysis, and tachycardia, as well as other symptoms consistent with neurotoxicity. Furthermore, in vitro studies have shown that Heloderma horridum venom inhibits ion flux and blocks the electrical stimulation of skeletal muscles. Helodermatids have long [...] Read more.
Bites from helodermatid lizards can cause pain, paresthesia, paralysis, and tachycardia, as well as other symptoms consistent with neurotoxicity. Furthermore, in vitro studies have shown that Heloderma horridum venom inhibits ion flux and blocks the electrical stimulation of skeletal muscles. Helodermatids have long been considered the only venomous lizards, but a large body of robust evidence has demonstrated venom to be a basal trait of Anguimorpha. This clade includes varanid lizards, whose bites have been reported to cause anticoagulation, pain, and occasionally paralysis and tachycardia. Despite the evolutionary novelty of these lizard venoms, their neuromuscular targets have yet to be identified, even for the iconic helodermatid lizards. Therefore, to fill this knowledge gap, the venoms of three Heloderma species (H. exasperatum, H. horridum and H. suspectum) and two Varanus species (V. salvadorii and V. varius) were investigated using Gallus gallus chick biventer cervicis nerve–muscle preparations and biolayer interferometry assays for binding to mammalian ion channels. Incubation with Heloderma venoms caused the reduction in nerve-mediated muscle twitches post initial response of avian skeletal muscle tissue preparation assays suggesting voltage-gated sodium (NaV) channel binding. Congruent with the flaccid paralysis inducing blockage of electrical stimulation in the skeletal muscle preparations, the biolayer interferometry tests with Heloderma suspectum venom revealed binding to the S3–S4 loop within voltage-sensing domain IV of the skeletal muscle channel subtype, NaV1.4. Consistent with tachycardia reported in clinical cases, the venom also bound to voltage-sensing domain IV of the cardiac smooth muscle calcium channel, CaV1.2. While Varanus varius venom did not have discernable effects in the avian tissue preparation assay at the concentration tested, in the biointerferometry assay both V. varius and V. salvadorii bound to voltage-sensing domain IV of both NaV1.4 and CaV1.2, similar to H. suspectum venom. The ability of varanid venoms to bind to mammalian ion channels but not to the avian tissue preparation suggests prey-selective actions, as did the differential potency within the Heloderma venoms for avian versus mammalian pathophysiological targets. This study thus presents the detailed characterization of Heloderma venom ion channel neurotoxicity and offers the first evidence of varanid lizard venom neurotoxicity. In addition, the data not only provide information useful to understanding the clinical effects produced by envenomations, but also reveal their utility as physiological probes, and underscore the potential utility of neglected venomous lineages in the drug design and development pipeline. Full article
(This article belongs to the Special Issue Drivers of Venom Potency across the Animal Kingdom)
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Figure 1
<p><span class="html-italic">Gallus gallus</span> chick biventer cervicis nerve–muscle preparation results after incubation with <span class="html-italic">Heloderma</span> venoms; (<b>A</b>) inhibition of indirect muscle twitches by <span class="html-italic">Heloderma exasperatum</span> (red), <span class="html-italic">H. horridum</span> (orange) and <span class="html-italic">H. suspectum</span> (purple) venoms relative to the initial twitches recorded prior to venom addition. Vehicle control shown in black; (<b>B</b>) effect of venoms on the contractile responses of the agonists acetylcholine (ACh), carbachol (CCh) and potassium chloride (KCl) relative to the initial response. All experiments were performed in triplicate.</p>
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<p>Binding affinity of <span class="html-italic">Heloderma</span> (<b>A</b>,<b>B</b>) and <span class="html-italic">Varanus</span> (<b>C</b>,<b>D</b>) crude venoms to the S3–S4 extracellular loop mimotope of domain IV of the human sodium channel Na<sub>V</sub>1.4. Figures (<b>A</b>,<b>C</b>) depict the area under the curve (AUC) of the curves displayed in figures (<b>B</b>,<b>D</b>). The Y axis of figure (<b>B</b>) shows the wavelength (nm) from the association (Ka binding) step. Asterisk symbols (*) above the bars (<b>A</b>,<b>C</b>) denote the level of statistical significance relative to the negative control. The negative control (-ve) was <span class="html-italic">Naja kaouthia</span> crude venom, while the positive control was <span class="html-italic">Leiurus quinquestriatus</span> crude venom. Dotted lines surrounding curves represent the error bars (<b>B</b>,<b>D</b>) based on SEM values from experiments performed in triplicate.</p>
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<p>Binding affinity of <span class="html-italic">Heloderma</span> (<b>A</b>,<b>B</b>) and <span class="html-italic">Varanus</span> (<b>C</b>,<b>D</b>) crude venoms to the S3–S4 extracellular loop mimotope of domain IV of the human calcium channel Ca<sub>V</sub>1.2. Figures (<b>A</b>,<b>C</b>) depict the area under the curve (AUC) of the curves displayed in (<b>B</b>) and (<b>D</b>). The Y axis of (<b>B</b>) shows the wavelength (nm) from the association (Ka binding) step. Asterisk symbols (*) above the bars (<b>B</b>,<b>D</b>) denote the level of statistical significance relative to the negative control. The negative control (-ve) was <span class="html-italic">Naja kaouthia</span> crude venom while the positive control was <span class="html-italic">Leiurus quinquestriatus</span> crude venom. Dotted lines surrounding curves (<b>C</b>,<b>D</b>) represent the error bars based on SEM values from experiments performed in triplicate.</p>
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<p>Graphic depicting the basic structure of a voltage-gated ion channel α-subunit displaying the position of the voltage-sensing domains I–IV in the phospholipid bilayer. Blue cylinders represent transmembrane helices while black lines represent connective loops. Highlighted in red is the S3–S4 extracellular loop of voltage-sensing domain IV used in the biolayer interferometry assays. As previously validated [<a href="#B57-toxins-13-00549" class="html-bibr">57</a>,<a href="#B80-toxins-13-00549" class="html-bibr">80</a>], biosensor mimotopes were designed from sequences for this region, as follows: for Ca<sub>V</sub>1.2 (Homo sapiens), AEHTQSSPSMNAEENSRISITFFRLFRVMRLVK, and for Na<sub>V</sub>1.4 (Homo sapiens), SIVGLALSDLIQKYFVSPTLFRVIRLARIGRVLR.</p>
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20 pages, 1174 KiB  
Article
Electrophysiological Properties from Computations at a Single Voltage: Testing Theory with Stochastic Simulations
by Michael A. Wilson and Andrew Pohorille
Entropy 2021, 23(5), 571; https://doi.org/10.3390/e23050571 - 6 May 2021
Cited by 4 | Viewed by 2543
Abstract
We use stochastic simulations to investigate the performance of two recently developed methods for calculating the free energy profiles of ion channels and their electrophysiological properties, such as current–voltage dependence and reversal potential, from molecular dynamics simulations at a single applied voltage. These [...] Read more.
We use stochastic simulations to investigate the performance of two recently developed methods for calculating the free energy profiles of ion channels and their electrophysiological properties, such as current–voltage dependence and reversal potential, from molecular dynamics simulations at a single applied voltage. These methods require neither knowledge of the diffusivity nor simulations at multiple voltages, which greatly reduces the computational effort required to probe the electrophysiological properties of ion channels. They can be used to determine the free energy profiles from either forward or backward one-sided properties of ions in the channel, such as ion fluxes, density profiles, committor probabilities, or from their two-sided combination. By generating large sets of stochastic trajectories, which are individually designed to mimic the molecular dynamics crossing statistics of models of channels of trichotoxin, p7 from hepatitis C and a bacterial homolog of the pentameric ligand-gated ion channel, GLIC, we find that the free energy profiles obtained from stochastic simulations corresponding to molecular dynamics simulations of even a modest length are burdened with statistical errors of only 0.3 kcal/mol. Even with many crossing events, applying two-sided formulas substantially reduces statistical errors compared to one-sided formulas. With a properly chosen reference voltage, the current–voltage curves can be reproduced with good accuracy from simulations at a single voltage in a range extending for over 200 mV. If possible, the reference voltages should be chosen not simply to drive a large current in one direction, but to observe crossing events in both directions. Full article
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Figure 1
<p>(<b>a</b>) Committor probabilities for Cl<math display="inline"><semantics> <msup> <mrow/> <mo>−</mo> </msup> </semantics></math> in p7 at <math display="inline"><semantics> <mrow> <mo>−</mo> <mn>140</mn> </mrow> </semantics></math> mV (red), <math display="inline"><semantics> <mrow> <mo>−</mo> <mn>70</mn> </mrow> </semantics></math> mV (green), <math display="inline"><semantics> <mrow> <mo>−</mo> <mn>35</mn> </mrow> </semantics></math> mV (black), 0 V (blue), 70 mV (cyan) and 140 mV (magenta). Error bars are shown for the N6 data sets at <math display="inline"><semantics> <mrow> <mo>−</mo> <mn>35</mn> </mrow> </semantics></math> mV and 140 mV; (<b>b</b>) Committor probabilities for p7 at 140 mV from the N6 data set for 1-sided forward (green) and backward (blue) trajectories, respectively, 2-sided data set in the backward direction (red lines), and average in the forward direction with error bars (red symbols). In the inset we show the number of first passage trajectories to reach <span class="html-italic">z</span> for one N6 data set in the forward (green) and backward (magenta) directions and the total (light blue).</p>
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<p>(<b>a</b>) PMFs for K<math display="inline"><semantics> <msup> <mrow/> <mo>+</mo> </msup> </semantics></math> (lower curves) and Cl<math display="inline"><semantics> <msup> <mrow/> <mo>−</mo> </msup> </semantics></math> (upper curves) in TTX from stochastic simulations with an applied voltage of 50 mV. The PMFs have been reconstructed by way of CWDM at the N6 (blue) and N7 (gold) levels or by way of CPM at the N6 (green) and N7 (magenta) levels; (<b>b</b>) PMF for Na<math display="inline"><semantics> <msup> <mrow/> <mo>+</mo> </msup> </semantics></math> in GLIC from stochastic simulations with applied voltage of 100 mV. The PMF has been reconstructed by way of CWDM at the N7 (blue) and N8 (gold) level or by way of CPM at the N7 (green) and N8 (magenta) level. In both panels, the underlying PMF is in red.</p>
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<p>(<b>a</b>) PMF for Cl<math display="inline"><semantics> <msup> <mrow/> <mo>−</mo> </msup> </semantics></math> in p7 from stochastic simulations with an applied voltage of 140 mV. The PMFs have been reconstructed by way of CWDM at the N6 (blue) and N7 (gold) levels or by way of CPM at the N6 (green) and N7 (magenta) levels. The input PMF (red) is shown for reference. PMFs at the N8 level are not shown, as they coincide with the underlying PMFs and statistical errors associated with this level arequite small and are poorly visible at this scale; (<b>b</b>) PMFs for P7 reconstructed by way of one-sided forward trajectories (green) using Equation (<a href="#FD13-entropy-23-00571" class="html-disp-formula">13</a>) and backward trajectories (blue) using Equation (<a href="#FD14-entropy-23-00571" class="html-disp-formula">14</a>) from stochastic simulations at the N6 level with applied voltage of 140 mV. Two-sided reconstruction (magenta) and the underlying PMF (red) are shown for comparison. Note that one-sided, but not two-sided reconstructions are burdened with large errors at the ends.</p>
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<p>(<b>a</b>) I-V curves for K<math display="inline"><semantics> <msup> <mrow/> <mo>+</mo> </msup> </semantics></math> (green) and Cl<math display="inline"><semantics> <msup> <mrow/> <mo>−</mo> </msup> </semantics></math> (blue) in TTX reconstructed from simulations at 50 mV at the N6 level. Blue and green dots are currents obtained from direct simulations at specific voltages.; (<b>b</b>) I-V curves for Cl<math display="inline"><semantics> <msup> <mrow/> <mo>−</mo> </msup> </semantics></math> in p7 reconstructed from simulations at 140 mV at the N6 (blue), N7 (green) and N8 (red) level, and for <math display="inline"><semantics> <mrow> <mo>−</mo> <mn>35</mn> </mrow> </semantics></math> mV at the N6 level (magenta). N7 and N8 curves are not shown because they are almost identical to the N6 results. Black dots are currents obtained from direct simulations at specific voltages. All reconstructions were done using the PMFs obtained by way of CPM. The results of reconstructions using the PMFs from CWDM are not displayed because they are nearly identical.</p>
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<p>I-V curves for Na<math display="inline"><semantics> <msup> <mrow/> <mo>+</mo> </msup> </semantics></math> in GLIC reconstructed from simulations at 100 mV at the N7 level with PMF from CPM (blue), at the N7 level with PMF from CWDM (magenta), and N8 with PMF from CWDM (red). N8 with CPM (not shown) is almost identical to N7 CPM. Black dots are currents obtained from direct simulations at specific voltages.</p>
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<p>Reconstructions of I-V curves in TTX from individual sets of trajectories for K<math display="inline"><semantics> <msup> <mrow/> <mo>+</mo> </msup> </semantics></math> (<b>a</b>) and Cl<math display="inline"><semantics> <msup> <mrow/> <mo>−</mo> </msup> </semantics></math> (<b>b</b>). The PMFs were obtained from CPM (upper panels) or CWDM (lower panels). The curves were calculated by way of Equation (<a href="#FD20-entropy-23-00571" class="html-disp-formula">20</a>) (blue) or Equation (<a href="#FD18-entropy-23-00571" class="html-disp-formula">18</a>) (green). All reconstructions were carried out from simulations at applied voltage of 50 mV at the N6 level. Note that blue curves, but not green curves, are tightly clustered together indicating that Equation (<a href="#FD20-entropy-23-00571" class="html-disp-formula">20</a>) is more accurate than Equation (<a href="#FD18-entropy-23-00571" class="html-disp-formula">18</a>).</p>
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14 pages, 2483 KiB  
Article
Potassium Efflux and Cytosol Acidification as Primary Anoxia-Induced Events in Wheat and Rice Seedlings
by Vladislav V. Yemelyanov, Tamara V. Chirkova, Maria F. Shishova and Sylvia M. Lindberg
Plants 2020, 9(9), 1216; https://doi.org/10.3390/plants9091216 - 16 Sep 2020
Cited by 20 | Viewed by 3005
Abstract
Both ion fluxes and changes of cytosolic pH take an active part in the signal transduction of different environmental stimuli. Here we studied the anoxia-induced alteration of cytosolic K+ concentration, [K+]cyt, and cytosolic pH, pHcyt, in [...] Read more.
Both ion fluxes and changes of cytosolic pH take an active part in the signal transduction of different environmental stimuli. Here we studied the anoxia-induced alteration of cytosolic K+ concentration, [K+]cyt, and cytosolic pH, pHcyt, in rice and wheat, plants with different tolerances to hypoxia. The [K+]cyt and pHcyt were measured by fluorescence microscopy in single leaf mesophyll protoplasts loaded with the fluorescent potassium-binding dye PBFI-AM and the pH-sensitive probe BCECF-AM, respectively. Anoxic treatment caused an efflux of K+ from protoplasts of both plants after a lag-period of 300–450 s. The [K+]cyt decrease was blocked by tetraethylammonium (1 mM, 30 min pre-treatment) suggesting the involvement of plasma membrane voltage-gated K+ channels. The protoplasts of rice (a hypoxia-tolerant plant) reacted upon anoxia with a higher amplitude of the [K+]cyt drop. There was a simultaneous anoxia-dependent cytosolic acidification of protoplasts of both plants. The decrease of pHcyt was slower in wheat (a hypoxia-sensitive plant) while in rice protoplasts it was rapid and partially reversible. Ion fluxes between the roots of intact seedlings and nutrient solutions were monitored by ion-selective electrodes and revealed significant anoxia-induced acidification and potassium leakage that were inhibited by tetraethylammonium. The K+ efflux from rice was more distinct and reversible upon reoxygenation when compared with wheat seedlings. Full article
(This article belongs to the Special Issue Plant Responses to Hypoxia)
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Graphical abstract

Graphical abstract
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<p>Changes of the free cytosolic K<sup>+</sup> concentration, [K<sup>+</sup>]<sub>cyt</sub>, in wheat (<b>a</b>) and rice (<b>b</b>) leaf protoplasts upon imposition of anoxia. Typical single traces in the presence of 10 mM K<sup>+</sup>, 1 mM Ca<sup>2+</sup> and pH 7.0 in the external medium.</p>
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<p>Anoxia-induced alterations of [K<sup>+</sup>]<sub>cyt</sub> in wheat and rice leaf protoplasts with and without tetraethylammonium (TEA, 1 mM, 30 min pre-incubation). Columns represent mean values ± SD. Values with different letters are significantly different at <span class="html-italic">p</span> &lt; 0.05, according to the Least Significant Difference LSD test.</p>
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<p>Changes of the free cytosolic H<sup>+</sup> concentration, pH<sub>cyt</sub>, in wheat (<b>a</b>) and rice (<b>b</b>) leaf protoplasts upon imposition of anoxia. Typical single traces.</p>
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<p>Anoxia-induced alterations of pH<sub>cyt</sub> in wheat and rice leaf protoplasts. Columns represent mean values ± SD. Values with different letters are significantly different at <span class="html-italic">p</span> &lt; 0.05, according to the LSD test.</p>
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<p>Effects of anoxia and tetraethylammonium (TEA, 0.1 mM) on the net uptake of K<sup>+</sup> by roots of intact wheat (<b>a</b>) and rice (<b>b</b>) seedlings. Negative values reflect potassium efflux. Arrows indicate the beginning of reoxygenation treatment (24 h). Mean values ± SD. Values with different letters are significantly different at <span class="html-italic">p</span> &lt; 0.05, according to the LSD test.</p>
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<p>Effects of anoxia on the pH of the incubation medium of wheat (<b>a</b>) and rice (<b>b</b>) seedlings. Mean values ± SD. Values with different letters are significantly different at <span class="html-italic">p</span> &lt; 0.05, according to the LSD test.</p>
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