• Journal of the Korean Institute of Electrical and Electronic Material Engineers
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• v.19 no.8
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• pp.724-731
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• 2006

We investigated the electrochemical properties for Langmuir-Blodgett (LB) films mixed with 4-octyl-4'-(5-carboxylpentamethyleneoxy)azobenzene (denoted as 8A5H) and phospholipid(L-a-dimyristoylphosphatidylcholine, denoted as DMPC and L-a-dilauroylphosphayidylcholine, denoted as DLPC). The LB films of 8A5H, 8A5H-DMPC and 8A5H-DLPC mixture monolayers were deposited by using the LB method on the indium tin oxide(ITO) glass. The electrochemical properties measured by using cyclic voltammetry with a three-electrode system, an Ag/AgCl reference electrode, a platinum wire counter electrode and LB film-coated ITO working electrode at various concentrations(0.1, 0.5, and 1.0 mol/L) of $NaClO_4$ solution. A measuring range was reduced from initial potential to -1350 mV, continuously oxidized to 1650 mV and measured to the initial point. The scan rates were 50, 100, 150 and 200 mV/s, respectively. As a result, LB films of 8A5H and 8A5H-DLPC mixture monolayers appeared irreversible process caused by only the oxidation current from the cyclic voltammogram and LB films of 8A5H-DMPC monolayer mixture was found to be caused by a reversible oxidation-reduction process.

• Journal of Life Science
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• v.20 no.9
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• pp.1332-1338
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• 2010

To elucidate the mechanism underlying the regulation of hST8Sia I gene expression in FenR-induced SH-SY5Y cells, we characterized the promoter region of the hST8Sia I gene. Functional analysis of the 5'-flanking region of the hST8Sia I gene showed that the -1146 to -646 region functions as the FenR-inducible promoter of hST8Sia I in SH-SY5Y cells. Site-directed mutagenesis indicated that the NF-&B binding site at -731 to -722 was crucial for the FenR-induced expression of hST8Sia I in SH-SY5Y cells. To investigate which signal transduction pathway was involved in FenR-stimulated induction of hST8Sia I in SH-SY5Y cells, we performed Western blot analysis using phospho-specific antibodies in order to measure their degree of regulatory phosphorylation. Phosphorylations of AKT and RelA (p65) subunit of NF-${\kappa}B$ were significantly elevated in cytosolic and nuclear fractions of FenR-stimulated SH-SY5Y cells, respectively, than in control or DMSO-treated SH-SY5Y cells. These results suggest that FenR induce transcriptional up-regulation of hST8Sia I gene expression through translocation of RelA (p65) subunit of NF-${\kappa}B$ to nucleus by AKT signal pathway in SH-SY5Y cells.

• International Journal of Industrial Entomology and Biomaterials
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• v.8 no.2
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• pp.189-194
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• 2004

Amylase isozyme based three multivoltine viz., N+p, Np, N+ $p^{cho}$ and two bivoltine-D6+p, D6p syngenic lines (Syn. L) were developed from germplasm (GP) stocks Nistari (N) and D6 respectively. haemolymph isozyme pattern at pH 7.0 and 8.5 depicted a total 11 number (Am $y_{1 to 6}$ at pH 7.0 and Am $y^{l to 5}$ at pH 8.5) of native proteins (NP) of various sizes are amylase isozyme expressers. Among eleven NPs, two NPs of 770 kDa (Am $y^{6}$ at pH 7.0) and 376 kDa (Am $y^3$ at pH 8.5) are $\alpha$-amylase expressers and remaining NPs of 370, 364, 350, 329 and 274 kDa at pH 7.0 and 206, 292, 416, 725 kDa at pH 8.5 are $\beta$-amylase expressers. Accordingly, digestive juice amylase isozyme pattern at aforesaid pH also depicted a total number of 10 NPs (Am $y^{1 to 5}$) at each pH 7.0 and 8.5 are amylase expressers of which NP of 387 kDa (Am $y^4$ at pH 7.0) and 780 kDa (Am $y^{5}$ at pH 8.5) are a-amylase expresser. Remaining NPs of 338,297 ＆ 216 kDa at pH 7.0 and 370, 341, 329 ＆302 kDa at pH 8.5 are $\beta$-amylase expresser. Recurrent backcross lines (RBL) viz., N+pRBL and NpRBL were developed through introgression of high shell weight character (a multigenic trait) to be used further for congenic line (Con. L) development and to understand any association with introgressed character. Isozyme pattern in haemolymph of RBLs depicted only one $\alpha$-amylase of 770 kDa at pH 7.0 and 376 kDa at pH 8.0 with three and four respective $\beta$-amylase bands but in bivoltine lines numbers of $\beta$-amylase bands vary between 1 to 2 at aforesaid pH. Variability was also observed in digestive juice of multivolitine and its RBLs but bivoltine lines express null activity at both pH except appearance of one very week $\alpha$-amylase band D6+p at pH 8.5. Overall study suggests that not a single NP at both pH is common for expression of any band of amylase isozyme i.e., a totally different set of proteins are the amylase isozyme expresser at specific pH and no molecular factor of amylase is associated in developed RBLs which showed improvement on survival, single cocoon shell weight (SCSW) and single filament length over receptor parents.s.s.s.

• Journal of the Korean Chemical Society
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• v.34 no.5
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• pp.490-497
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• 1990

Two synthetic routes for the 1,4-diboracyclohexene-2 ring 8 have been developed. Method i) starts with 1,2-bis(dichloroaluminyl)ethane, in which the AlCl$_2$ group is replaced by BCl$_2$. Exchange of the chlorine with BI$_3$ in 1,2-bis-(dichloroboryl)ethane yields the corresponding iodo compound, which reacts with the alkynes to heterocycles 8a, b in good yield. In method ii) B$_2$Cl$_4$ is added to alkenes, replacement of chlorine with BI$_3$ yields the bis(diiodoboryl)ethane derivatives which undergo redox reactions with alkynes to give 8c, d. The diiodo derivative 8a forms the pyridine adduct 9a, and reacts with ether to give the ethoxy derivative 8f. 8a-d react with AlMe$_3$ to yield the corresponding dimethyl derivatives 8g-j, which give unstable radical anions when treated with potassium in THF. The ESR parameters are reported. In electrochemical experiments irreversible reductions of 8g-j are observed. 8g-j react with (C$_5$H$_5$)Co(C$_2$H$_4$)$_2$ to give the intermediate 16 VE complexes (C$_5$H$_5$)Co(8), in which C-H activation occurs with formation of the corresponding red 1,4-diboracyclohexadiene complexes 10. The X-ray structure analyses of 10h and 10j are reported.

• Journal of Life Science
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• v.14 no.6 s.67
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• pp.1009-1017
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• 2004

Sialyltransferases cloned so far show the remarkable tissue-specific expression, which is correlated with the existence of cell type-specific sialylated sugar structure in glycoconjugates. In the previous studies, we found various mRNA isoforms of human sialyltransferases generated by alternative splicing and alternative promoter utilization. To understand the regulatory mechanisms for specific expression of human sialyltransferase genes and for production of their mRNA isoforms, in this study, we have isolated and characterized five kinds of human sialyltransferase genes: hST3Gal II, hST8Sia II, hST8Sia III, hST8Sia IV, and hST8Sia V. The hST3Gal II gene is composed of six exons, which span over 17kb, with exons ranging in size from 46 to over 1017 bp. The hST8Sia III gene comprises over 10 kb, and consists of only four exons, which is much smaller and simpler than other human sialyltransferase genes. In contrast, three genes (hST8Sia II, hST8Sia IV and hST8Sia V) span more than 70 kb, and comprise five or more exons. All exon-intron boundaries follow the GT-AG rule. In particular, the sialylmotif L, which is a highly conserved region in all cloned sialyltransferases, was found in one exon of hST8Sia III, whereas this motif is encoded by discrete exons in the other human sialyltransferases. Exon structures of these sialyltransferase genes show the structural diversity, as found in other human sialyltransferase genes reported so far. We determined the transcription start site of hST3Gal II gene by the 5'-RACE and cap site hunting experiments.

• Journal of the Korean Society of Food Science and Nutrition
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• v.34 no.10
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• pp.1638-1641
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• 2005

In order to develop novel food products or additives using transglutaminase (TGase), some physicochemical and morphological understandings are needed. Raw skim milk was adjusted to pH 5.5, 7.0, and 8.5, and each was treated with microbial TGase for 0, 1, 2, 4, and 8 hours, for the protein structure observation using scanning electron microscope (SEM), The particles of untreated raw skim milk were small and evenly associated. After adjustment of pH to 5.5 and treatment of TGase for 1-hour, the protein particles aggregated widely in a bigger form than that of control. Under the same condition for 2 hours, the particles associated and clustered. The particles gathered widely and became a number of small spherical forms after 4 hours. After 8 hours, they made larger forms than the result of 1-hour treatment, and the aggregation broadened. Under the pH 7.0 and 8.5 conditions with TGase-treatment, the protein Particles fractionated and associated into the bigger masses at 1 hour point, but each piece slowly became smaller and more fractionated until treated time reached 4 hours. After 8 hours, the fragmented protein particles aggregated into larger forms as those on the pH 5.5 condition. In general, the electron microscopical forms of the samples adjusted to pH 5.5 showed smaller than those of pH 7.0 or pH 8.5, It is suggested that the protein particles and textural behavior were influenced by pH, TGase, and reaction time.

• Archives of Pharmacal Research
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• v.23 no.1
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• pp.31-34
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• 2000

An efficient procedure for the preparation of 7,8-dichloro-6-nitro-1H-1,5-benzodiazepine-2,4-(3H, 5H)-dione(7) as a potential lead compound for the NMDA receptor glycine binding site antagonist, starting from readily available 4,5-dichloro-2-nitroaniline(8), is described. The key step in the synthesis involves the cyclization of malonic ester amide 10 to compound 11.

• Corrosion Science and Technology
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• v.7 no.1
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• pp.40-44
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• 2008

Passive metal forms an interfacial diffuse layer on the surface of passive film by its reaction with $H^+$ or $OH^-$ ions in solution depending on solution pH. There is a critical pH, called pH point of iso-selectivity ($pH_{pis}$) at which the nature of the diffuse layer is changed from the anion-permeable at pH<$pH_{pis}$ to the cation-permeable at pH>$pH_{pis}$. The $pH_{pis}$ for a passivated Fe was determined by examining the effects of pH on the thickness of passive film and on the dissolution reaction occurring on the passive film under a gavanostatic reduction in borate-phosphate buffer solutions at various pH of 7~11. The steady-state thickness of passive film formed on Fe showed the maximum at pH 8.5~9, and further the nature of film dissolution reaction was changed from a reaction producing $Fe^{3+}$ ion at $pH\leq8.5$ to that producing $FeO_2{^-}$ at $pH\geq9$, suggesting that the $pH_{pis}$ of Fe is about pH 8.5~9. In addition, the passive film formed at pH 8.5~9, $pH_{pis}$, was found to be the most protective with the lowest defect density as confirmed by the Mott-Schottky analysis. Pitting potential was decreased with increasing $Cl^-$ concentration at $pH\leq8.5$ due probably to the formation of anion permeable diffuse layer, but it was almost constant at $pH\geq9$ irrespective of $Cl^-$ concentration due primarily to the formation of cation permeable diffuse layer on the film, confirming again that $pH_{pis}$ of Fe is 8.5~9.

• KSBB Journal
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• v.11 no.2
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• pp.193-200
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• 1996

In molecular biology, type-II restriction endonuclease, which specifically recognize and cleave DNA at a limited number of sites, have been exploited as a means of characterizing DNA fragments, DNA mapping for genetic engineering. Type-II restriction endonucleases have been found to modulate their substrate specificity under modified conditions such as extreme pH, ionic strength, high enzyme concentration, substitution of metallic cofactors or addition of organic solvents. This study was initiated to investigate the modification of recognition specificity of BamHI according to the different pH and organic solvent under the given buffer condition. The specificity of BamHI is highly depends on the presence of hydrophobicity (LogP: partition coefficient) and pH of reaction solution. The specificity of BamHI is changed in range of LogP -1.03∼-1.35(at pH 7.5), -1.03∼-2.5 (at pH 8.0), -0.75∼-0.25(at pH 8.5), 0.32∼-2.5(at pH 8.9), respectively. Alteration of specificity appears in lower concentration of organic solvent when the reaction occurs in more alkali pH. For example, in DMSO solution, alteration of specificity appears in 20% concentration at pH 7.5 but in 4% concentration at pH 8.9.

• Bulletin of the Korean Chemical Society
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• v.32 no.7
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• pp.2428-2432
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• 2011

A series of new 4-aryl-6,8-dimethylpyrimido[4,5-c]pyridazine-5,7(6H,8H)-diones have been synthesized via three component reaction of 1,3-dimethylbarbituric acid with arylglyoxals in the presence of hydrazinium dihydrochloride in ethanol. All of these derivatives may act as potential monoamine oxidase inhibitors.