• Economic and Environmental Geology
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• v.29 no.4
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• pp.421-428
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• 1996

The occurrence, optical property, chemical composition, crystal structure and formation environments of the phillipsite within deep-sea manganese nodules were systematically investigated in this study. Phillipsite in manganese nodules occurs in nucleus of nodules along with consolidated bottom sediments, weathered volcanic debris, and interstitial grains in the each layer of manganese encrusts. Phillipsite is predominantly pseudomorphs of volcanic shards, and occurs as white to pale yellow in color lath-shaped and equant crystals. These show aggregations of prismatic, blocky, and bladed of 2 to $20{\mu}m$ long, and 2 to $5{\mu}m$ thick. The simplified average chemical formula of phillipsite is $({Ca_{0.1}Mg_{0.3}Na_{1.1}K_{1.5}})_3{(Fe_{0.3}Al_{4.2}Si_{11.8})O_{32}{\cdot}10H_2O}$ with a very siliceous and alkalic. The $Si/(Al+Fe^{+3})$ ratio is 2.37 to 2.78 and alkalis greatly exceed the divalent exchangeable cations, and Na/K ratio is 0.59 to 0.81. The phillipsite is monoclinic ($P2_l/m$) with the unit-cell parameters, $a=10.005{\AA}$, $b=14.129{\AA}$, $c=8.686{\AA}$, ${\beta}=124.35^{\circ}$, and $V=1013.6{\AA}^3$. Phillipsites in manganese nodules formed apparently authigenically at a temperature less than $10^{\circ}C$, and they crystallized at a pressure of less than 0.7 kb, and pH of about 8 in deep-sea environments.

• Korean Journal of Veterinary Research
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• v.38 no.1
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• pp.29-42
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• 1998

$Mg^{2+}$ is one of the most abundant divalent cations in mammalian body(0.2~1.0mM) and the important physiological roles are : first, the cofactor of many enzyme activities, second, the regulator of glycolysis and DNA synthesis, third, the important role of bioenergetics by regulating of phosphorylation, fourth, the influence of cardiac metabolism and function. In this work we have investigated the regulation of the $Mg^{2+}$ induced by ${\alpha}_1-adrenoceptor$ stimulation in perfused guinea pig hearts and isolated myocytes. The $Mg^{2+}$ content of the perfusate or the supernatant was measured by atomic absorbance spectrophotometry. The elimination of $Mg^{2+}$ in the medium increased the force of contraction of right ventricular papillary muscles, and the left ventricular pressure. Phenylephrine also enhanced the force of contraction in the presence of $Mg^{2+}-free$ medium. ${\alpha}_1-Agonists$ such as phenylephrine and methoxamine were found to induce $Mg^{2+}$ efflux in both perfused hearts and myocytes. These effects were blocked by prazosin, an ${\alpha}_1-adrenoceptor$ antagonist. The $Mg^{2+}$ influx could also be induced by phenylephrine and R59022, a diacylglycerol kinase inhibitor. In the presence of protein kinase C(PKC) inhibitors, phenylephrine produced an increase in $Mg^{2+}$ efflux from perfused hearts. Furthermore, $Mg^{2+}$ efflux by phenylephrine was amplified by phorbol 12-myristate 13-acetate(PMA). This enhancement of $Mg^{2+}$ efflux by PMA was blocked by prazosin in perfused hearts. By contrast, the $Mg^{2+}$ influx could be induced by verapamil, nifedipine, ryanodine in perfused hearts, but not in myocytes. $W^7$, a $Ca^{2+}$/calmodulin antagonist, completely blocked the phenylephrine-induced $Mg^{2+}$ efflux in perfused hearts. In conclusion, $Mg^{2+}$ is responsible for the cardiac activity associated with ${\alpha}_1-adrenoceptor$ stimulation. The mobilization of $Mg^{2+}$ is decreased or increased by ${\alpha}_1-adrenoceptor$ stimulation in guinea pig hearts. These responses may be related specifically to the respective pathways of signal transduction. A decrease in $Mg^{2+}$ efflux by ${\alpha}_1-adrenoceptor$ stimulation in hearts can be through PKC dependent and intracellular $Ca^{2+}$ levels.

• Journal of the Mineralogical Society of Korea
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• v.23 no.3
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• pp.235-242
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• 2010

Froth flotation using the residual water in the end of flotation process has been performed through controlling of pH. IEP (isoelectric point) of molybdenite and quartz in distilled water was below pH 3 and pH 2.7, respectively and the stabilized range was pH 5~10. In case of a suspension in reusing water, zeta potential of molybdenite decreased to below -10 mV or less at over pH 4 due to residual flocculants. As result of pH control, flotation efficiency in the alkaline conditions was deteriorated by flocculation, resulting from expanded polymer chain, ion bridge of the divalent metal cations ($Ca^{2+}$), and hydrophobic interactions between the nonpolar site of polymer/the hydrophobic areas of the particle surfaces. However, the weak acid conditions (pH 5.5~6) improved the efficiency of flotation as hydrogen ions neutralize polymer chains and then weakened its function. In cleans after rougher flotation, the Mo grade of 52.7% and recovery of 90.1% could be successfully obtained under the conditions of 20 g/t kerosene, 50 g/t AF65, 300 g/t $Na_2SiO_3$, pH 5.5 and 2 cleaning times. Hence, we developed a technique which can continuously supply waste water filtered from tailings into the grinding-rougher-cleaning processes.

• Proceedings of the Botanical Society of Korea Conference
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• 1987.07a
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• pp.133-148
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• 1987

Gibberellin(GA) 3-$\beta$ hydroxylation is very important for the shoot elogation in the higher plants, since only 3$\beta$-hydryoxylated GAs promote shoot elogation in several plants. Fluctuation of 3$\beta$-hydryoxylase activity was examined during seed maturation using two cultivars of , P. vulgaris, Kentucky Wonder (normal) and Masterpiece (dwarf). Very immature seeds of both cultivars contain high level of 3$\beta$-hydroxylase activity (per mg protein). Both cultivars showed maximum of enzyme activity (per seed) in the middle of their maturation process. Gibberellin 3$\beta$-hydroxylase catalyzing the hydroxylation of GA20 to GA1 was purified 313-fold from very early immature seeds of P. vulgaris. Crude soluble enzyme extracts were purified by 15% methanol precipitation, hydrophobic interaction chromatogrphy, DEAE ion exchange column chromatography and gel filtration HPLC. The 3$\beta$-hydroxylase activity was unstable and lost much of its activity duting the purification. The molecular weight of purified enzyme was extimated to be 42, 000 by gel filtration HPLC and SDS-PAGE. The enzyme exhibited maximum activity at pH 7.7. The Km values for [2.3-3H] GA20 and [2.3-3H]GA9 were 0.29 $\mu$M and 0.33 $\mu$M, respectively. The enzyme requires 2-oxoglutarate as a cosubstrate; the Km value for 2-oxoglutarate was 250 $\mu$M using 3H GA20 as a substrate. Fe2+ and ascorbate significantly activated the enzyme at all purification steps, while catalase and BSA activated the purified enzyme only. The enzyme was inhibited by divalent cations Mn2+, Co2+, Ni2+, Cu2+, Zn2+, Cd2+ and Hg2+. Effects of several GAs and GA anaogues on the putrified 3$\beta$-hydroxylase were examined using [3H]GA9 and GA20 as a substrates. Among them, GA5, GA9, GA15, GA20 and GA44 inhibited the enzyme activity. [13C, 3H] GA20 was converted by the partially purified enzyme preparation to [13C, 3H]GA1, GA5 and GA6, which were identified by GC-MS, GA9 was converted only GA4, GA15 and GA44 were converted to GA37 and GA38, respectively. GA5 was epoxidized to GA6 by the preparation. This suggests that 3$\beta$-hydroxylation of GA20 and epoxidation of GA5 are catalyzed by the same enzyme in P, vulgaris.

• Microbiology and Biotechnology Letters
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• v.12 no.4
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• pp.277-283
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• 1984

In the forward reaction (ADP formation) of the adenylate kinase from baker's yeast, dissociation constants from binary complexes are higher by a factor of about 4 times then those from at ternary complexes. In the reverse reaction, dissociation constants from the binary complexes are 2 times higher then those from the ternary complexes. The enzyme showed activities against various nucleotide triphospate in following orders; ATP 100, UTP 18, ITP 9 and GTP 5, of the necleotide monophosphate. only dAMP showed 33% activity of that AMP as phosphate acceptor. Divalent cations were required in enzyme reaction in following orders; $Mg^{2＋}$ 100, Co$^{2＋}$ 57, Mn$^{2＋}$ 54, $Ca^{2＋}$ 51, Ni$^{2＋}$ 10 and Sn$^{2＋}$ 6. AMP, as a substrate inhibitor, competitively inhibited the adenylate kinase at pH 7.2 or 8.0. Inhibition constants of the enzyme showed greater dependence on the pH of the reaction mixture, which was the lower Ki values under higher pH. Adenosine pentaphospho adenosine was competive inhibitor to the enzyme against all substrate, and it showed the same Ki values, 2.9mM. Further, PEP was competive inhibitor with respect to AMP and non-competive inhibitor with respect to MgATP. Adenylate kinase from bakers yeast was similar to mitochondrial type of animal in the contents of aianine, leucine and asparagine or asparatic acid differing from muscle type enzyme. Based on the results and observation, characteristic of yeast adenylate kinase resembled the adenylate kinase of mitochondrial type from animals. Further, difference of characteristics in adenylate kinasa depending upon the workers might be due to the difference of strain used.

• Nutritional Sciences
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• v.9 no.1
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• pp.20-28
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• 2006

Aryl sulfotransferase (AST) IV is a liver enzyme involved in detoxication and has been shown to be susceptible to down regulation by a number of hepatotoxic xenobiotics. Studies presented here to investigate the ability of biological and non-biological divalent metal cations on AST IV activity showed that AST IV was strongly inhibited following in vitro or in vivo exposure to. Zn ( II ), Co ( II ) or Cd ( II ). It was found that $0.025\sim$2.5 uM of these metal ions were sufficient to cause $50\%$ of inhibition in vitro in purified AST IV and $0.25\sim$25 uM of these metal ions in liver cytosolic fractions. For the in vivo study, 1,000 mg Cu ( II )/kg, 2,000 mg Zn ( II )/kg or 250 mg Cd( II )/kg was added to individual diets and administered to three (3) group; of mts over a 7 week period The Co ( II )-supplemented diet produced no apparent change in rat growth rate and resulted in 30-fold increase in liver cytotolic Cu ( II ) levels, suggesting that elevated levels of Cu ( II ) ion in the liver were responsible for the loss of AST IV activity. In contrast, the Zn ( II )-supplemented diet caused a decrease in rat growth rates and resulted in zero increase in liver Zn ( II ) levels, which suggested an indirect inhibition mechanism was caused by Zn ( II ) in the liver. Rats were fed the Cd-supplemented diet also displayed a decrease in growth rate with little or no change in liver Cu ( II ) or Zn ( II ) levels. When the liver cytosols of mts from the metal ion diets were immunochemically analyzed for the AST IV and albumin contents, no significant changes were observed in albumin levels. However, AST IV contents in the cytosols of mts fed the Zn ( II )-supplemented diets showed a slight decrease in amount These results showed that AST IV activity in vitro and in vivo can be inhibited by Co ( II ), Zn ( II ), and Cd ( II ) by apparently different mechanisms. The immediate response to a Zn injection showed a decrease in AST IV activity but not in the AST IV content in liver cytosol. These mechanisms appeared to involve direct actions of the metal ion on AST IV activity and indirect actions affecting AST IV amount.

• Microbiology and Biotechnology Letters
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• v.47 no.3
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• pp.434-440
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• 2019

Lactic acid bacteria (LAB) isolated from kimchi were studied for their ${\beta}$-glucuronidase activity. Among the 156 strains tested, 52 strains utilized glucuronic acid as a carbon source and their intracellular ${\beta}$-glucuronidase activities were significantly higher than their extracellular activities. Leuconostoc mesenteroides KFRI 73007 isolated from turnip kimchi exhibited the highest intracellular ${\beta}$-glucuronidase activity of $0.77{\pm}0.01U/mg$ protein, which was further increased to $1.14{\pm}0.01U/mg$ protein under optimized reaction conditions (pH 7, $37^{\circ}C$). The activity of ${\beta}$-glucuronidase was notably decreased by the addition of divalent cations, and glucuronic acid was the best carbon source to produce ${\beta}$-glucuronidase in Leu. mesenteroides KFRI 73007.

• The Korean Journal of Physiology
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• v.23 no.2
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• pp.237-252
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• 1989

Effect of a $Na^+$ gradient on $Ca^{2+}$ uptake was studied in isolated sarcolemmal vesicles of cat ileal longitudinal muscle. $Ca^{2+}$ uptake was markedly stimulated in the presence of an outwardly directed $Na^+$ gradient. External $Na^+$, monensin and A23187 abolished the $Na^+-dependent$ $Ca^{2+}$ uptake. Monovalent cations such as $K^+$, $Li^+$, $Rb^+$, $Cs^+$ and choline could not substitute for $Na^+$ in enhancement of $Ca^{2+}$ uptake. Divalent cations such as $Ba^{2+}$, $Sr^{2+}$, $Mn^{2+}$ and $Cd^{2+}$ but not $Mg^{2+}$ inhibited the $Na^+-dependent$ $Ca^{2+}$ uptake. Increase in external pH in the range of 6.0 to 8.0 stimulated the $Na^+-dependent$ $Ca^{2+}$ uptake. Amiloride inhibited the $Na^+-dependent$ $Ca^{2+}$ uptake at concentrations above 0.5 mM, whereas diltiazem or vanadate did not. The apparent Km of the $Na^+-dependent$ $Ca^{2+}$ uptake for $Ca^{2+}$ was 18.2 ${\mu}M$ and apparent Vmax was 689.7 pmole/mg protein/5 sec. Kinetic analysis of the $Na^+-dependent$ $Ca^{2+}$ uptake showed a noncompetitive interaction between internal $Na^+$ and external $Ca^{2+}$. The dependence of $Ca^{2+}$ uptake on internal $Na^+$ showed sigmoidal kinetics and Hill coefficient for internal $Na^+$ was 2.52. Inside positive membrane potential generated by imposing an inwardly directed $K^+$ gradient and valinomycin significantly stimulated the $Na^+-dependent$ $Ca^{2+}$ uptake. These results indicate that a $Na^+-Ca^{2+}$ exchange system exists in the sarcolemmal membranes isolated from cat ileal longitudinal muscle and it might operate as an electrogenic process.

• Korean Journal of Soil Science and Fertilizer
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• v.20 no.2
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• pp.153-159
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• 1987

Adsorption and desorption characteristics of $^{42}K$ and $^{45}Ca$ were studied by making use of the natural zeolite, bentonite, and vermiculite. The work included that the fittness tests for the Freundlich and the Langmuir adsorption isotherms and desorption of the radionuclides from adsorbents by extracting with $NH^+_4$ ($1N-NH_4OAc$). The adsorption by the radionuclides are fitted well with both of the adsorption equations. The Langmuir adsorption maximum of $^{42}K$ is higher than that of $^{45}Ca$ by the zeolite and bentonite except vermiculite, and the values of $^{42}K$ decrease in the order of Zeolite (Zt)>Bentonite (Bt)>Vemiculite (Vt). As for $^{45}Ca$, the maximum adsorption values decrease in the order of Bt>Vt>Zt. The ionic radii of K and Ca seem to be closely related with fixation in the cavity of the zeolite that adsorb more $^{42}K$ than $^{45}Ca$. The smaller ionic size of Ca seems to be resulted in the lower adsorption of $^{45}Ca$ by the zeolite because Ca could leave easily from the cavity. Ionic size of K, however, seems to be similar with size of the cavity. $^{45}Ca$ adsorption by the bentonite, on the other hand, show higher adsorption than $^{42}K$. The higher charge density of the divalent cations than those of the monovalent cations seems to be the main consideration. For the retention strength of the adsorbed $^{42}K$ and $^{45}Ca$ by the adsorbents, a comparison is made by use of the Langmuir constant(k). The results indicated that the constant values for K are smaller than those of Ca in all the adsorbents. It seems that the smaller values of the constant, the weaker retention strength. For $^{42}K$, the percentage of desorption decrease in the order of Zt>Bt>Vt, but in the case of $^{45}Ca$, it decreases in the order of Vt>Zt>Bt. The results show that the weaker binding strength as represented by small value of the Langmuir constant, the higher percentage of the removal except fixing preferably $K^+$ by the vemiculite. In conclusion, the zeolite could adsorb much more $^{42}K$ and remove it more than others. For $^{45}Ca$, the bentonite could adsorb more and desorb less than others.

• Progress in Medical Physics
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• v.14 no.1
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• pp.54-67
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• 2003

The voltage-dependence of N-type calcium current inactivation is U-shaped with the degree of inactivation roughly mirroring inward current. This voltage-dependence has been reported to result from a purely voltage-dependent mechanism. However, $Ca^{2＋}$-dependent inactivation of N-channels has also been reported. We have investigated the role of $Ca^{2＋}$ in N-channel inactivation by comparing the effects of $Ba^{2＋}$and $Ca^{2＋}$ on whole-cell N-current in rat superior cervical ganglion neurons. For individual cells in-activation was always larger in $Ca^{2＋}$ than in $Ba^{2＋}$ even when internal EGTA (11 mM) was replaced with BAPTA (20 mM). The inactivation vs. voltage relationship was U-shaped in both divalent cations. The enhancement of inactivation by $Ca^{2＋}$ was inversely related with the magnitude of inactivation in $Ba^{2＋}$ as if the mechanisms of inactivation were the same in both $Ba^{2＋}$ and $Ca^{2＋}$. In support of this idea we could separate fast ( ${\gamma}$ ～150 ms) and slow ( ${\gamma}$ ～ 2500 ms) components of inactivation in both $Ba^{2＋}$and $Ca^{2＋}$ using 5 sec voltage steps. Differential effects were observed on each component with $Ca^{2＋}$ enhancing the magnitude of the fast component and the speed of the slow component. The larger amplitude of fast component indicates that the more channels inactivate via this pathway with $Ca^{2＋}$ than with $Ba^{2＋}$, but the stable time constants support the idea the fast inactivation mechanism is identical in $Ba^{2＋}$and $Ca^{2＋}$. The results do not support a $Ca^{2＋}$-dependent mechanism for fast inactivation. However, the $Ca^{2＋}$-induced acceleration of the slowly inactivating component could result from a $Ca^{2＋}$-dependent process.