• Clean Technology
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• v.13 no.1 s.36
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• pp.64-71
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• 2007

The selection of a suitable adsorbent for removing organic sulfur compounds tetrahydrothiophene (THT) and t-butylmercaptan (TBM) from natural gas has been carried out. The saturation adsorption capacity for the sulfur compounds were determined by pulse adsorption method for a group of nanoporous materials, including Na-Y, Na-ZSM-5, Na,K-ET(A)S-10, Na-Mordenite, Na,K-Clinoptitolite, Ti/MCM-41, Ti/SBA-15 and amorphous titanosilicates. Among the materials tested, Na-Y and Na,K-ET(A)S-10 zeolites showed high adsorptive capacities for THT and TBM. The saturation capacity for THT on Na,K-ETS-10 was comparable with that on Na-Y zeolite, which is well known as an effective adsorbent. The capacity and adsorptivity for THT and TBM on Na,K-ETAS-10 were improved by an increase in crystallinity of Na,K-ETAS-10. An investigation of the competitive adsorption between THT and TBM from the breakthrough test using a simulated natural gas indicates that Na,K-ETS-10 selectively adsorbs THT. The breakthrough capacity for THT on Na,K-ETS-10 was 1.19 mmol/g. The results show that the high adsorption performance of Na.K-ETS-10 and Na,K-ETAS-10 is due to the highly exchanged cations in the zeolitic structure which exhibit the strong electrostatic interactions with organic sulfur compounds and their wide pore nature.

• Korean Journal of Environmental Agriculture
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• v.17 no.3
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• pp.215-219
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• 1998

This experiment was conducted to investigate effects of NaCl concentration on photosynthetic rate, free proline content and ion content in tobacco. As NaCl concentration was increased growth was retarded. The decrease growth characteristics(shoot/root ratio was 2.0) at 90mM NaCl indicated that this concentration could be a limiting level. As NaCl concentration was increased photosynthetic rate, transpiration rate, and water use efficiency were decreased. Photosynthetic rate was highly decreased at 60mM NaCl. There was no significant difference between transpiration rate and water use efficiency. Leaf water potential was decreased as NaCl concentration was increased, in that twice lower at 30mM than that of control and drop largely at 120mM NaCl. Free proline content was increased as NaCl increased until 120mM NaCl and drop at 150mM NaCl. The $Ca^{2+}$, $Mg^{2+}$, and $K^+$ contents were increased until NaCl concentration was 120mM. The $Na^{2+}$ content was slowly increased as NaCl concentration increased until 120mM NaCl, and largely increased at 150mM NaCl. There was no significant difference between $Cl^-$ and NaCl treatments except 30 mM NaCl in which $Cl^-$ content was higher than that of control. As NaCl concentration was increased $K^+/Na^+$ ratio was decreased. The negative correlation between $K^+$ and $Na^+$, and positive correlation between $K^+/Na^+$ and protein content were found.

• Journal of Radiation Protection and Research
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• v.14 no.1
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• pp.1-7
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• 1989

In order to evalulate the cause of polyuric acute tubular necrosis, we measured electrolytes, $Na^{+}\;and\;K^{+}$ excreted in urine, and activities of $Na^{+}-K^{+}$adenosine triphosphatase ($Na^{+}-K^{+}$ATPase) Excretion of $Na^{+}\;and\;K^{+}$ significantly increased in 24hr exposure on the uranyl nitrate and then decreased below the normal level after 3 days. The concentration of $Na^{+}\;and\;K^{+}$ in urines of the rats treated uranyl nitrate was less than that of the normal rats. The activities of $Na^{+}-K^{+}$ATPase decreased only in the group treated with high dose group of uranyl nitrate (30mg/kg BW) on the 3rd day but were not changed in the low dose groups(5 mg/kg BW and 15mg/kg BW).

• The Korean Journal of Zoology
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• v.38 no.4
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• pp.449-456
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• 1995

Seasonal changes in the activity and charaderistics of brain Na+, K+-ATPase and Mg2+-AWase were investigated in frog (Rana dybowskii) The brain Na+, K+-ATPase adivity during hibernation was similar to that in active period in frogs. The Na+, K+-AWase activity increased in December and March, when the frogs enter into and awake from the hibernation. Over 5-35$^{\circ}C$ temperature range, Na+, K+-ATPase showed non4inear Arrhenius kinetics throughout the year. The brain Mg2+-ATPase activity decreased during hibernation, but markedly increased in March. The Arrhenius plots for Mg2+-AWase activity were linear in frogs both in torpid and active state. The ratio of Na+, K+-AWase activity at 15~C to at 35~C did not change during hibernation. The sensitivity of Na+, K+-AWase to ouabain was also unchanged throughout the year. These results indicate that the activity and charaderistics of brain Na+, K+-AWase remain unchanged during hobernadon in frog.

• Korean Journal of Soil Science and Fertilizer
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• v.40 no.1
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• pp.64-70
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• 2007

In this experiment we transformed the Ca-bentonite into Na-bentonite with two inorganic Na-chemicals under different temperatures. These two Na-chemicals were selected among five different Na-chemicals which carries Na as cation. The swelling capacity of the Na chemical-treated bentonite was increased with increasing Na concentration, while the maximum concentration of Na solution decreased with increasing temperature. $Na_2CO_3$ was most effective in exchanging Ca ions and resulting in the highest swelling index among the Na-chemicals. The swelling index was significantly increased with increasing temperature to $100^{\circ}C$. But the equilibration time reversely affected the swelling index due to a rapid increase in evaporation of water. Within same amount of Na treatment SI slightly decreased not only with increasing contacting time but also with increasing temperature. The adsorption for the transformed Na-bentonite was increased with increasing equilibrium concentrations of Pb and Cd ions for all the activated Na-B and indigenous Ca-B and Na-B while the adsorbability of $Pb^{2+}$ onto each Na-B sample is more than that of $Cd^{2+}$. And the maximum adsorption capacity sequence of Na-B samples for Pb and Cd has been found to be 5 % $Na_2CO_3.$ - 5 % $NaHCO_3$ > 3 % $NaHCO_3$ > 3 % $Na_2CO_3$ > 1 % $NaHCO_3$ > 1 % $Na_2CO_3$ > indigenous Na-B > indigenous Ca-B, showing that there are contradictory results about the relationship of cation adsorption to CEC.

• The Korean Journal of Physiology
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• v.17 no.2
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• pp.161-168
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• 1983

Studies on the effects of vanadate for Na-K-ATPase activity were carried out with rabbit renal cortex. 1) Na-K-ATPase activity was inhibited with the concentrations of vanadate in incubation medium. The vanadate concentration at which activity was inhibited by 50%$(ID_{50})$ was $10^{-6}M$ and Hill coefficient was 1.00. 2) The fractional inhibition by constant concentration of vanadate decreased with increasing enzyme concentration. 3) Increasing $K^+$ and $Na^+$ concentrations in incubation medium diminished the ability to inhibit Na-K-ATPase by vanadate whereas increasing $K^+$ and $Mg^{2+}$ concentrations potentiated the inhibition of Na-K-ATPase by vanadate. 4) Vanadate didn't inhibit Na-K-ATPase at pH 6.6. Increasing pH potentiated the inhibition of Na-K-ATPase activity. 5) Vanadate inhibited Na-K-ATPase activity reversibly in all range of concentrations in dilution experiment. These results show that vanadate inhibits Na-K-ATPase activity with interacting at $KE_2$ state reversibly.

• The Korean Journal of Pharmacology
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• v.26 no.1
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• pp.35-49
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• 1990

A highly purified $(Na^+,\;K^+)-ATPase$ from the rectal gland of Squalus acanthias and from the electric organ of Electrophorus electricus has been used to raise antibodies in rabbits. The 97,000 dalton catalytic subunit and glycoprotein derived from the rectal gland of spiny shark were also used as antigens. The two $(Na^+,\;K^+)-ATPase$ holoenzymes and the two shark subunits were antigenic. In Ouchterlony double diffusion experiments, these antibodies formed precipitation bands with their antigens. Antibodies prepared against the two subunits of shark holoenzyme also formed precipitation bands with their antigens and shark holoenzyme, but not with eel holoenzyme. These observations are in good agreement with inhibitory effect of these antibodies on the catalytic activity of $(Na^+,\;K^+)-ATPase$ both from the shark and the eel, since there is very little cross-reaction between the shark anticatalytic subunit antibodies and the eel holoenzyme. The maximum antibodies titer of the anticatalytic subunit antibodies is found to be 6 weeks after the initial single exposure to this antigen. Multiple injections of the antigen increased the antibody titer. However, the time required to produce the maximum antibody titer was approximately the same. These antibodies also inhibit catalytic activity of $(Na^+,\;K^+)-ATPase$ vesicles reconstituted by a slow dialysis of cholate after solubilization of the enzyme in a presonicated mixture of cholate and phospholipid. In these reconstituted $(Na^+,\;K^+)-ATPase$ vesicles, effects of these antibodies on the fluxes of $Na^+$, $Rb^+$, and $K^+$ were investigated. Control or preimmune serum had no effect on the influx of $^{22}Na^+$ or the efflux of $^{86}Rb^+$. Immunized sera against the shark $(Na^+,\;K^+)-ATPase$ holoenzyme, its glycoprotein or catalytic subunit did inhibit the influx of $^{22}Na^+$ and the efflux of $^{86}Rb^+$. It was also demonstrated that these antibodies inhibit the coupled counter-transport of $Na^+$ and $K^+$ as studied by means of dual labeling experiments. However, this inhibitory effect of the antibodies on transport of ions in the $(Na^+,\;K^+)-ATPase$ vesicles is manifested only on the portion of energy and temperature dependent alkali metal fluxes, not on the portion of ATP and ouabain insensitive ion movement. Simultaneous determination of effects of the antibodies on ion fluxes and vesicular catalytic activity indicates that an inhibition of active ion transport in reconstituted $(Na^+,\;K^+)-ATPase$ vesicles appears to be due to the inhibitory action of the antibodies on the enzymatic activity of $(Na^+,\;K^+)-ATPase$ molecules incorporated in the vesicles. These findings that the inhibitory effects of the antibodies specific to $(Na^+,\;K^+)-ATPase$ or to its subunits on ATP and temperature sensitive monovalent cation transport in parallel with the inhibitory effect of vesicular catalytic activity by these antibodies provide direct evidence that $(Na^+,\;K^+)-ATPase$ is the molecular machinery of active cation transport in this reconstituted $(Na^+,\;K^+)-ATPase$ vesicular system.

• Toxicological Research
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• v.5 no.2
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• pp.79-87
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• 1989

Changes in urinary $Na^+$ and $K^+$ excretions, renal cortical microsomal $Na^+$ -K-ATPase activity, cortical tissue electrolyte content and plasma aldosterone level were studied in rats treated with CdCl2 (2 mg Cd/kg/day, s.c. injection) for 7-14 days. After 7 days of cadmium exposure, urinary excretion of $Na^+$ was markedly reduced. This change was accompanied by an increase in $Na^+$-$K^+$-ATPase activity, a fall in tissue $Na^+$ content, a rise in tissue $K^+$ content and an elevation of plasma aldosterone level.

• Journal of Mushroom
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• v.3 no.2
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• pp.65-70
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• 2005

This study was carried out to select oyster mushroom strains tolerant to salinity and characteristic cultivation by different NaCl concentration. Among the 64 strains, Kimjae-10ho, Nongki-2-1ho, Myungyul, Byungneutari-1ho, Bupyungsoyae-1ho, Sambok and Chunchu-2ho resulted in higher mycelial growth and density on PDA medium containing NaCl. The maxium NaCl concentration possible to fruit body formation was 0.5% NaCl in Myungyul, 1.0% NaCl in Kimjae-10ho and Bupyungsoyae-1ho, 1.5% NaCl in Nongki-2-1ho, Byungneutari-1ho, Sambok and Chunchu-2ho, respectively. Increased NaCl concentration on sawdust medium prolonged culture period, while decreased total quantity and come to be short and thin in Length and thickness of stipe. Higher NaCl concentration in the medium decreased the uptake rate of $K_2O$ and CaO, whereas increased the NaCl uptake rate.

• Archives of Pharmacal Research
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• v.21 no.6
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• pp.707-711
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• 1998

The (Na,K)ATPase is responsible for generating the ionic gradients and membrane potentials by the exchange of intracellular $Na^+$ for $K^+$. It has been recentl y shown that (Na,K)ATPase is involved in the exocytic pathway of basic fibroblast growth factor (bFGF), although it is not known that bFGF is secreted to the outside of cell through direct interaction with (Na,K) ATPase. To understand the role for (Na,K)ATPase in the secretary pathway of bFGF, we have sought to identify the cytoplasmic domains of the alpha1 isoform of (Na,K)ATPase interacting with bFGF by yeast two-hybrid system. We have also investigated the interaction between the alpha2 isoform of (Na,K)ATPase and bFGF to find out whether the interaction is isoform-specific. We found that none of the cytoplasmic domains of (Na,K)ATPase isoforms interacted with bFGF. The result suggests that the interaction between bFGF and (Na,K)ATPase might be indirect, thus requiring other proteins which are involved in the formation of protein complexes for the interaction, although we cannot exclude the possibility that the interaction requires the element of the whole alpha subunit structure that was not present in the isolated alpha subunit cytoplasmic domains.