• Bulletin of the Korean Chemical Society
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• v.16 no.12
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• pp.1176-1179
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• 1995

1H NMR spectra of pyridine, α-, β-, and γ-picoline coordinated to the paramagnetic heteropolyanion [Ni3(PW9O34)2]12- (P2Ni3) are reported. NMR lines are assigned to [Ni3(ptl)n(PW9O34)2]12- (n=1, 2 or 3; ptl=pyridine-type ligand) on the basis of their [P2Ni3]/[ptl] dependence. The formation constants for γ-picoline complexes at 25 ℃ are K1=80, K2=610, and K3=190 L mol-1. The monopicoline complex has greater affinity for γ-picoline than P2Ni3. A degradation product, [Ni2(WO2)(PW9O34)2]12-, was also identified at low pH by measuring the NMR spectrum of pyridine coordinated to it. The isotropic NMR shifts come mainly from the contact interaction due to σ-electron delocalization.

• Journal of Life Science
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• v.18 no.8
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• pp.1159-1163
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• 2008

The purpose of this study was to establish a high-throughput assay method capable of estimating specific lipase activity at oil-water interface. The method is based on the fact that fluorescence intensity of fluorescein is affected by pH. The pH-dependence might be used to monitor pH change caused by the release of fatty acid through the action of lipase. Assay was performed by incubating a reaction mixture containing oil emulsion, fluorescein and enzyme and by monitoring fluorescence intensity periodically. Fluorescence intensity decreased linearly with a rate proportional to the enzyme amount. Linear relationship was observed between enzyme amount and reaction rate which was calculated from a graph of fluorescence change against time. The assay was possible at different pH conditions in the range of pH 6.0-8.0.

• Journal of the Korean Vacuum Society
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• v.6 no.1
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• pp.61-68
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• 1997

We examined the dependence of the growth of undoped InP epilayer by chloride vapor phase epitaxy on the growth temperature and on the $PCl_3$molar fraction. The growth temperature was varied from $620^{\circ}C$ to $650^{\circ}C$ and the $PCl_3$molar franction from $2.5{\times}10^{-2}$ to $4.5{\times}10^{-2}$. The undoped InP epilayer with hillock free surface was obtained at the growth temperature of $640^{\circ}C$ and at the PCl$_3$molar fraction of $3.0{\times}10^{-2}$. The surface morphology was improved with a decrease of the PCl$_3$molar fraction. The carrier concentration measured by Hall and ECV was less than $1{\times}10^{14}cm^{-3}$. The resistivity of the undoped InP epilayer, measured by using four probe method, showed a high value of <$3.0{\times}10^6{\Omega}\textrm{cm}$.

• Microbiology and Biotechnology Letters
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• v.43 no.3
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• pp.300-305
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• 2015

The glutamate decarboxylase gene (gadB) from Lactobacillus plantarum WCFS1 was cloned and expressed as an N-terminal hexa-histidine-tagged fusion protein in Escherichia coli BL21 (DE3) as the host strain. Purified glutamate decarboxylase (GAD) was immobilized onto porous silica beads by covalent coupling. The pH dependence of activity and stability of the immobilized GAD was significantly altered, when compared to those of the free enzyme. Immobilized GAD was stable in the range of pH 3.5 to 6.0. The resulting packed-bed reactor produced 41.7 g of γ-aminobutyric acid/l·h at 45℃.

• Journal of the Korean Magnetics Society
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• v.5 no.5
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• pp.524-527
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• 1995

The temperature dependence of spin wave mode separation in amorphous $Co_{89.5}Zr_{10.5}$ thin film has been investigated at temperatures between 100 K and 300 K. The magnetization and the spectroscopic splitting factor were obtained for the main resonance mode in parallel and perpendicular magnetic field. ${\Delta}H_{2-3}$, the difference between resonance field of mode 2 and the resonance field of mode 3, increases with decreasing temperature. The linewidth increases for all the modes with decreasing temperature. Especially in mode 3 it increases rapidly below 200 K. This phenomenon could be caused by the increase of exchange stiffness constant or the decrease of surface magnetic anisotropy constant with decreasing temperature.

• Bulletin of the Korean Chemical Society
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• v.25 no.5
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• pp.601-602
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• 2004

• Bulletin of the Korean Chemical Society
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• v.15 no.11
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• pp.1001-1003
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• 1994

A series of phosphodiesters of p-nitrophenyl phosphoryl derivatives were synthesized and used as a model substrate for phospholipase D (PLD). The phosphodiester substrates were synthesized from p-nitrophenyl phosphorodichloridate and corresponding alcohols with different chain lengths and polar groups. To measure the activity of PLD, either spectroscopic method for p-nitrophenol or pH-stat titration method was employed. For each substrate, effects of substrate concentration, pH, and $Ca^{2+}$ ion were examined. The kinetic parameters $V_{max}$ for the different substrates were varied depending on the chain lengths or charge of the alcohols. No calcium effect was observed in the hydrolysis of neutral and negatively charged alcohol derivatives, while positively charged choline derivative showed a strong $Ca^{2+}$ ion dependence.

• Journal of Pharmaceutical Investigation
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• v.32 no.1
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• pp.1-6
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• 2002

The mucoadhesive characteristics of [P(AA-co-PEGMM)] films by estimating the glass transition temperature $(T_g)$, analyzing surface energy and studying FT-IR was previously reported. In this study, the possibility of buccal mucoadhesive dosage form of [P(AA-co-PEGMM)] films by mucoadhesive force measurements and dissolution tests were also investigated. Mucoadhesiveness of [P(AA-co-PEGMM)] films was compared with cr-PAA and cr-PEGMM films crosslinked with 3% ethyleneglycol dimethacrylate (EGDMA). The buccal mucoadhesive force of [P(AA-co-PEGMM)] films increased with increasing content of PEGMM. [P{AA-co-PEGMM (18 mole%)}] films showed a significantly greater mucoadhesiveness than cr-PAA and cr-PEGMM films. The mucoadhesive force measured in normal saline (pH 5.0) was higher than that measured in phosphate buffer (pH 6.8) because of the pH dependence of hydrogels with carboxyl ions within the PAA. Moreover, the mucoadhesive force of [P{AA-co-PEGMM (18 mole%)}] films was at maximum after 2 hr attachment of buccal mocosa and it was maintained over $1\;N/cm^2$ for up to 10 hr. In dissolution studies, the release of butorphanol tartrate from [P(AA-co-PEGMM)] films increased with increasing PEGMM content, and films prepared with 18 mole% PEGMM gave almost zero order release kinetics.

• Archives of Pharmacal Research
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• v.29 no.8
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• pp.677-684
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• 2006

Morphine has been used widely on the treatment of many types of chronic pain. However the development of tolerance to and dependence on morphine by repeat application is a major problem in pain therapy. The purpose of the present study was to investigate whether combined administration of nalbuphine with morphine affects the development of tolerance to and dependence on morphine. We hypothesize that the use of nalbuphine, ${\kappa}-agonist$ may prove to be useful adjunct therapy to prevent morphine-induced undesirable effects in the management of some forms of chronic pain. Morphine (10 mg/kg) was injected to rats intraperitoneally for 5 day. The variable dose of nalbuphine (0.1, 1.0 and 5.0 mg/kg) was administered (i.p.) in combination with morphine injection. The development of morphine tolerance was assessed by measuring the antinociceptive effect with the Randall-Selitto apparatus. The development of dependence on morphine was determined by the scoring the precipitated withdrawal signs for 30 min after injection of naloxone (10 mg/kg, i.p.). Nalbuphine did not attenuate antinociceptive effect of morphine in rats. Interestingly, combined administration of morphine with nalbuphine (10:1) significantly attenuated the development of dependence on morphine. The elevation of $[^3H]MK-801$ binding in frontal cortex, dentate gyrus, and cerebellum after chronic morphine infusion was suppressed by the coadministration of nalbuphine. In addition, the elevation of NR1 expression by morphine was decreased by the coadministration of nalbuphine in rat cortex. These results suggest that the coadministration of nalbuphine with morphine in chronic pain treatment can be one of therapies to reduce the development of tolerance to and dependence on morphine.

• Applied Biological Chemistry
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• v.50 no.4
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• pp.257-261
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• 2007

Tolaasin, a peptide toxin produced by Pseudomonas tolaasii, causes a serious disease on the cultivated mushrooms, known as brown blotch disease. Hemolysis using red blood cells was designed to measure the cytotoxicity of tolaasin molecules. Since tolaasin has two amine groups near the C-terminus, its membrane binding will be dependent on the ionic states of the amine groups. When the tolaasin peptide was titrated, its titration curve indicated the presence of titratable amine(s) at pH ranges from 7.0 to 9.6. When the pH-dependence of tolaasin-induced hemolysis was measured at various pHs, hemolysis was more efficient at alkaline pHs. In order to measure the membrane binding activity of tolaasin at different pHs, RBCs were incubated with tolaasin molecules for short time periods and washed out with fresh buffer. Because of the tolaasin binding during the preincubation period, fast hemolyses were observed at pH 8 or higher. These results imply that non-charged or less positively charged states of tolaasin molecules easily bind to membrane and show high hemolytic activity.