scholarly journals NH4+ Currents across the Peribacteroid Membrane of Soybean. Macroscopic and Microscopic Properties, Inhibition by Mg2+, and Temperature Dependence Indicate a SubpicoSiemens Channel Finely Regulated by Divalent Cations

2005 ◽  
Vol 139 (2) ◽  
pp. 1015-1029 ◽  
Author(s):  
Gerhard Obermeyer ◽  
Stephen D. Tyerman
Keyword(s):  
Temperature Dependence ◽  
Divalent Cations ◽  
Peribacteroid Membrane

The temperature dependence of ionic influences on contractile function in frog twitch muscle

1980 ◽  
Vol 58 (1) ◽  
pp. 74-84 ◽  
Author(s):  
J. G. Foulks ◽  
Lillian Morishita
Keyword(s):  
Temperature Dependence ◽  
Skeletal Muscles ◽  
Time Course ◽  
Contractile Function ◽  
Divalent Cations ◽  
Organic Anion ◽  
Ionic Composition ◽  
Amino Groups ◽  
Chloride Solutions ◽  
Reduced Temperature

Alterations in the ionic composition of the medium produce striking changes in the potential-dependent contractile responses of skeletal muscles. This study was undertaken to examine the temperature dependence of some of these effects. The suppression of maximal K contractures of frog toe muscles in media lacking divalent cations was largely overcome by a sufficient increase in temperature. The restoration of K contractures by perchlorate in the absence of divalent cations was prevented by a sufficient decrease in temperature. The effect of perchlorate was to shift the temperature dependence of these contractures toward lower temperatures. The reduction in the amplitude of maximal K contractures in the absence of divalent cations was less marked after pretreatment with a reagent (trinitrobenzenesulfonate) that selectively modifies free amino groups, although the temperature dependence of these contractures was unchanged. The reduction in the amplitude of K contractures in the presence of an organic anion (hexanoate) was partially antagonized both by an increase in temperature or by a decrease in temperature, effects that resemble those observed in solutions in which the divalent cation concentration was reduced. In chloride solutions, the relation between [K]0 and K contractures was shifted toward lower [K]0 by an increase in temperature, whereas in perchlorate solutions increased temperature produced a shift in the opposite direction. The shift in this relation toward lower [K]0 at reduced temperature, and the accelerated time course of K contractures with an increase in temperature were similar in perchlorate and in chloride solutions. Thermodynamic analysis by Arrhenius plots indicated that the influence of divalent cations and perchlorate anions on K contractures may be the result of their effects on hydrational factors.

Thermodynamics of Ag0-Solvation in Molten Silver Halides, Doped with Metal Halides

1985 ◽  
Vol 40 (2) ◽  
pp. 131-136
Author(s):  
Konrad G. Weil
Keyword(s):  
Temperature Dependence ◽  
Thermodynamic Functions ◽  
Divalent Cations ◽  
Metal Halides ◽  
Silver Halides ◽  
Breaking Effect ◽  
Structure Breaking

From the temperature dependence of the solubility of silver in its molten halides, the thermodynamic functions ΔHsolv and ΔSsolv are calculated. They depend strongly on the presence and concentration of mono- and divalent cations. A possible structure breaking effect of these ions is discussed.

Ultrastructural Localization of Acid Mucosubstance in Skeletal Muscle

1967 ◽  
Vol 25 ◽  
pp. 52-53 ◽  
Author(s):  
William J. Dougherty ◽  
Samuel S. Spicer
Keyword(s):  
Striated Muscle ◽  
Divalent Cations ◽  
Ultrastructural Localization ◽  
Major Elements ◽  
Frozen Sections ◽  
Thorium Dioxide ◽  
Iron Solution ◽  
Coupling System ◽  
Psoas Muscles ◽  
Formalin Fixed

In recent years, considerable attention has focused on the morphological nature of the excitation-contraction coupling system of striated muscle. Since the study of Porter and Palade, it has become evident that the sarcoplastic reticulum (SR) and transverse tubules constitute the major elements of this system. The problem still exists, however, of determining the mechamisms by which the signal to interdigitate is presented to the thick and thin myofilaments. This problem appears to center on the movement of Ca++ions between myofilaments and SR. Recently, Philpott and Goldstein reported acid mucosubstance associated with the SR of fish branchial muscle using the colloidal thorium dioxide technique, and suggested that this material may serve to bind or release divalent cations such as Ca++. In the present study, Hale's iron solution adapted to electron microscopy was applied to formalin-fixed myofibrils isolated from glycerol-extracted rabbit psoas muscles and to frozen sections of formalin-fixed rat psoas muscles.

Temperature Dependence of the Critical Electron Dose for Fatty Acid Monolayers

1982 ◽  
Vol 40 ◽  
pp. 78-79
Author(s):  
Kenneth H. Downing ◽  
Robert M. Glaeser
Keyword(s):  
Electron Beam ◽  
Fatty Acid ◽  
Inelastic Scattering ◽  
Temperature Dependence ◽  
Structural Damage ◽  
Direct Result ◽  
Second Step ◽  
Strong Temperature Dependence ◽  
Electron Dose ◽  
Covalent Bonds

The structural damage of molecules irradiated by electrons is generally considered to occur in two steps. The direct result of inelastic scattering events is the disruption of covalent bonds. Following changes in bond structure, movement of the constituent atoms produces permanent distortions of the molecules. Since at least the second step should show a strong temperature dependence, it was to be expected that cooling a specimen should extend its lifetime in the electron beam. This result has been found in a large number of experiments, but the degree to which cooling the specimen enhances its resistance to radiation damage has been found to vary widely with specimen types.

Temperature Dependence of Magnetic Domains and Wall Structures

1972 ◽  
Vol 30 ◽  
pp. 496-497
Author(s):  
Sonoko Tsukahara ◽  
Tadami Taoka ◽  
Hisao Nishizawa
Keyword(s):  
Temperature Dependence ◽  
Domain Walls ◽  
Magnetic Domain ◽  
Iron Film ◽  
Objective Lens ◽  
Lorentz Microscopy ◽  
Domain Structures ◽  
Wall Structures ◽  
Crystal Films ◽  
Metallurgical Structure

The high voltage Lorentz microscopy was successfully used to observe changes with temperature; of domain structures and metallurgical structures in an iron film set on the hot stage combined with a goniometer. The microscope used was the JEM-1000 EM which was operated with the objective lens current cut off to eliminate the magnetic field in the specimen position. Single crystal films with an (001) plane were prepared by the epitaxial growth of evaporated iron on a cleaved (001) plane of a rocksalt substrate. They had a uniform thickness from 1000 to 7000 Å.The figure shows the temperature dependence of magnetic domain structure with its corresponding deflection pattern and metallurgical structure observed in a 4500 Å iron film. In general, with increase of temperature, the straight domain walls decrease in their width (at 400°C), curve in an iregular shape (600°C) and then vanish (790°C). The ripple structures with cross-tie walls are observed below the Curie temperature.

Structure, assembly and interactions of the nuclear lamina and the nuclear pore complex

1992 ◽  
Vol 50 (1) ◽  
pp. 490-491
Author(s):  
N. Panté ◽  
M. Jarnik ◽  
E. Heitlinger ◽  
U. Aebi
Keyword(s):  
Nuclear Pore Complex ◽  
Divalent Cations ◽  
Nuclear Lamina ◽  
Dynamic Structure ◽  
Nucleocytoplasmic Transport ◽  
Nuclear Pore ◽  
Cytoplasmic Filaments ◽  
Radial Spokes ◽  
Nuclear Ring ◽  
Central Plug

The nuclear pore complex (NPC) is a ∼120 MD supramolecular machine implicated in nucleocytoplasmic transport, that is embedded in the double-membraned nuclear envelope (NE). The basic framework of the ∼120 nm diameter NPC consists of a 32 MD cytoplasmic ring, a 66 MD ‘plug-spoke’ assembly, and a 21 MD nuclear ring. The ‘central plug’ seen in en face views of the NPC reveals a rather variable appearance indicating that it is a dynamic structure. Projecting from the cytoplasmic ring are 8 short, twisted filaments (Fig. 1a), whereas the nuclear ring is topped with a ‘fishtrap’ made of 8 thin filaments that join distally to form a fragile, 30-50 nm distal diameter ring centered above the NPC proper (Fig. 1b). While the cytoplasmic filaments are sensitive to proteases, they as well as the nuclear fishtraps are resistant to RNase treatment. Removal of divalent cations destabilizes the distal rings and thereby opens the fishtraps, addition causes them to reform. Protruding from the tips of the radial spokes into perinuclear space are ‘knobs’ that might represent the large lumenal domain of gp210, a membrane-spanning glycoprotein (Fig. 1c) which, in turn, may play a topogenic role in membrane folding and/or act as a membrane-anchoring site for the NPC. The lectin wheat germ agglutinin (WGA) which is known to recognize the ‘nucleoporins’, a family of glycoproteins having O-linked N-acetyl-glucosamine, is found in two locations on the NPC (Fig. 1. d-f): (i) whereas the cytoplasmic filaments appear unlabelled (Fig. 1d&e), WGA-gold labels sites between the central plug and the cytoplasmic ring (Fig. le; i.e., at a radius of 25-35 nm), and (ii) it decorates the distal ring of the nuclear fishtraps (Fig. 1, d&f; arrowheads).

Effects of Mg2+ on Chromatic Structure in Isolated Chicken Liver Nuclei

1990 ◽  
Vol 48 (3) ◽  
pp. 130-131
Author(s):  
Soichiro Arai ◽  
Yuh H. Nakanishi
Keyword(s):  
Chromatin Structure ◽  
Room Temperature ◽  
Osmium Tetroxide ◽  
Divalent Cations ◽  
Chromatin Condensation ◽  
Chicken Liver ◽  
Electron Microscopic ◽  
Razor Blade ◽  
Microscopic Studies ◽  
Liver Nuclei

Although many electron microscopic studies on extracted chromatin have provided considerable information on chromatin condensation induced by divalent cations, there is only a little literature available on the effects of divalent cations on chromatin structure in intact nuclei. In the present study, the effects of Mg2+ on chromatin structure in isolated chicken liver nuclei were examined over a wide concentration range of Mg2+ by scanning electron microscopy.Nuclei were prepared from chicken liver by the method of Chauveau et al. with some modifications. The nuclei were suspended in 25 mM triethanolamine chloride buffer (pH7.4) with 1 mM EDTA or in the buffer with concentrations of MgCl2 varying from 1 to 50 mM. After incubation for 1 min at 0°C, glutaraldehyde was added to 1.8% and the nuclei were fixed for 1 h at 4°C. The fixed nuclei were mixed with 15% gelatin solution warmed at about 40°C, and kept at room temperature until the mixture set. The gelatin containing the nuclei was fixed with 2% glutaraldehyde for 2-4 h, and cut into small blocks. The gelatin blocks were conductive-stained with 2% tannic acid and 2% osmium tetroxide, dehydrated in a graded series of ethanol, and freeze-cracked with a razor blade in liquid nitrogen.

Temperature dependence of generation-recombination noise in p-n junctions

2002 ◽  
Vol 12 (3) ◽  
pp. 71-74
Author(s):  
J. A. Jiménez Tejada ◽  
A. Godoy ◽  
A. Palma ◽  
P. Cartujo
Keyword(s):  
Temperature Dependence
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