• Title/Summary/Keyword: molecular bands

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New Red Phosphor with the Improved Color Purity for PDP Applications

  • Mho, Sun-Il
    • 한국정보디스플레이학회:학술대회논문집
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    • 2002.08a
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    • pp.257-259
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    • 2002
  • As a new host material for a red phosphor for PDP applications, has studied (Y,Gd)$Al_3(BO_3)_4$ which gives non-centrosymmetric sites for $Eu^{3+}$ activators. Vacuum ultraviolet (VUV) excitation spectrum of new red phosphor (Y,Gd)$Al_3(BO_3)_4$:$Eu^{3+}$ has two broad bands. One band with the absorption edge at ca. 168 nm is the band-gap absorption of aluminoborate and the other broad band centered 240 nm is the charge transfer transition between $Eu^{3+}$ and the neighboring oxygen anions. The PL spectrum shows the strongest emission at 617 nm due to the electric dipole $^5D_0{\rightarrow}^7F_2$ transition of $Eu^{3+}$, whose luminescent chromaticity is (0.67, 0.33).

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STRUCTURAL ANALYSIS OF COPPER PHTHALOCYANINE THIN FILMS FABRICATED BY PLASMA-ACTIVATED EVAPORATION

  • Kim, Jun-Tae;Jang, Seong-Soo;Lee, Soon-Chil;Lee, Won-Jong
    • Journal of Surface Science and Engineering
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    • v.29 no.6
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    • pp.851-856
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    • 1996
  • Copper Phthalocyanine (CuPc) thin films were fabricated on the silicon wafers by plasma activated evaporation method and structural analysis were carried out with various spectroscopies. The CuPc films had dense and smooth morphology and they also showed good mechanical properties and chemical resistance. The main molecular structure of the CuPc, which is the conjugated aromatic heterocyclic ring structure, was maintained even in the plasma process. However, metal-ligand (Cu-N) bands were deformed by the plasma process and the structure became amorphous especially at higher process pressures. Oxygen impurities were incorporated in the film and carboxyl functional groups were formed at the peripheral benzene ring. The structure and morphology of the films were dependent on the process pressure but relatively irrespective of the RF power.

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Purification and Characterization of the Recombinant Bacillus pasteurii Urease Overexpressed in Escherichia coli

  • Shin, In-Seon;Lee, Mann-Hyung
    • Journal of Microbiology and Biotechnology
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    • v.9 no.3
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    • pp.255-259
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    • 1999
  • A 6.9-kb DNA fragment including the minimal Bacillus pasteurii urease gene cluster was subcloned into a high-copy-number plasmid vector, pUC19, and the recombinant B. pasteurii urease was overexpressed in Escherichia coli. The recombinant urease was purified 25.9-fold by using combinations of anion-exchange and gel-filtration chromatography followed by Mono-Q chromatography on a FPLC. N-terminal peptide sequencing analyses revealed that two distinct smaller peptide bands resolved on a 10-18% gradient SDS-PAGE corresponded to UreA and UreB peptides, respectively. It was also shown that the ureB gene was translated from a GUG codon and the first methionine residue was post-translationally cleaved off. The native molecular weight of the recombinant urease was 176,000 and 2 nickel atoms were present per catalytic unit. pH stability studies of the purified enzyme showed that the recombinant Bacillus pasteurii urease is stable in alkaline pH range, which is similar to the enzyme of the evolutionarily related bacterium, Sporosarcina ureae.

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Characterization of an antimicrobial Chitinase Purified from the Grapefruit Extract (자몽 추출물로부터 분리된 항균성 Chitinase의 특성)

  • 김외연;정나은;제대엽;이동철;김재원;조성환;이상열
    • Korean Journal Plant Pathology
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    • v.10 no.4
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    • pp.277-283
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    • 1994
  • An antimicrobial chitinase was purified from grapefruit extract and its properties were characterized. The chitinase was purified with a single step chromatography on regenerated chitin affinity gel column. The molecular weight of the purified chitinase was 29 kDa. The grapefruit extract contained the chitinase protein more than 50% of its total soluble proteins measured by coomassie stained protein bands. When the purified chitinase was incubated with polymers of N-acetylglucosamine (NAG), such as mycelia of Fusarium oxysproum and swollen chitin, they were degraded to oligosaccharides, and the oligosaccharides were then further hydrolyzed by the same enzyme to monomer and dimer of NAG. This result suggests that the chitinase contained both endo- and exo- chitinase activities. The chitinase was stable to heat and pH treatment; its activity was not diminished by the heat treatment upto 7$0^{\circ}C$ for 1 hr, and it showed a pH stability in the range of pH 4.0 to 12.0.

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Charge Transfer between Graphene and a Strong Electron Acceptor, Tetrafluorotetracyanoquinodimethane (F4-TCNQ)

  • Lee, Ji-Eun;Kim, Seon-Ho;Gang, Seong-Gyu;Yang, Seong-Ik;Ryu, Sun-Min
    • Proceedings of the Korean Vacuum Society Conference
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    • 2011.02a
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    • pp.458-458
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    • 2011
  • Graphene, a single atomic layer of sp2-bonded carbon, shows substantial potential for various applications. Chemical manipulation of its electronic properties will be of great importance. In this study, we have investigated interaction between graphene and organic molecular layer of tetrafluorotetracyanoquinodimethane (F4-TCNQ), a strong electron acceptor. F4-TCNQ films of varying thickness were evaporated onto graphene mechanically exfoliated on SiO2/Si substrates. F4-TCNQ molecules increase the frequencies of Raman G and 2D bands of graphene while decreasing the linewidth of G band and 2D/G intensity ratio, which is consistent with increase of hole density in graphene. These results exemplify the possibility of chemical tuning of electronic properties of graphene.

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Restriction pattern of the nucleic acid of Synechococcus sp. cyanophage

  • Park, Jong-Geun;Kim, Min;Choi, Yong-Keel;Yoon, Sung-Nyo
    • Journal of Microbiology
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    • v.34 no.1
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    • pp.1-6
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    • 1996
  • The nucleic acid of Synechococcus sp. cyanophage was identified as double-stranded DNA by the result of digestion with enzymes such as exonucleases, DNase, and S1 nuclease, and by acridine orange staining. The cyanophage DNA was cleaved with several restriciton ehdonucleases such as ApaI, BamHI, Bg/II, HaeIII, Eco RI, HindIII, PstI, AND aPAI gave the clearest sets of bands on agarose gels and the fragment numbers for each were 12, 20, 29, 20, and 7, respectively. The sums of the size from Bam HI and PstI digestions were estimated approximately 227$\pm$4 kb, which are in agreement with the result of the pulsed field gel electrphoresis. This virus is thought to have the largest genosome among those of known cyanophages, which corresponds to the largest haed ot 90 nm when compared with the head sizes of cyanophages discovered since 1963.

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Studies of Density-Fractionated Human Ervthrocvte Membranes (농도분배에 따라 분리한 사람 적혈구 막에 관한 연구)

  • 정종문
    • The Korean Journal of Zoology
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    • v.37 no.4
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    • pp.597-604
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    • 1994
  • Membranes obtained from the normal human RBC population were separated by continuous sucrose density gradient centrifugation and the density-fractionated membranes were then examined for changes in molecular markers. This study focuses on changes of (i) the membrane protein profile, (ii) differences in membrane-associsted enzyme activities, and (iii) the amount of autologous IgG bound. The following observations were made: (i) ratios for band 4. la over the sum of bands (4. la + 4.Ib) ranged from 0.58 to 0.79 for membranes of lowest density; (ii) significant changes in bound glyceraldehyde-3-phosphate dehydrogenase and acetvlcholinesterase activities were found; (iii) the amounts of autolosous IgG's attached to the red blood cells was highest in the membrane fraction of lowest density.

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Purification and Properties of Protein Methylase I from Hog Pancreas (돼지 췌장내 Protein Methylase I의 분리정제 및 성질)

  • 이향우;장만식
    • YAKHAK HOEJI
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    • v.31 no.3
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    • pp.173-181
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    • 1987
  • Protein methylase I has been partially purified from hog pancreas with a 11% yeild. The final preparation is completely free of any other protein-specific methyltransferases and endogenous substrate proteins. The enzyme has an optimum pH of 7.2 and the approximate molecular weight is above 800 thousands dalton. The Km values for S-adenosyl-L-methionine and histone type II-A are 1.32$\times$10$^{-5}$M. The Ki value for S-adenosyl-L-homocysteine is 1.52$\times$10$^{-6}$M. The effect of enyzme concentration on the activity showed a slight sigmoidal curve suggesting the involvement of certain cofactors. Even though the purified enzyme showed two bands on polyacrylamide gel electrophoresis, the enzyme is highly specific for the arginine residues of protein and specifically, highly specific for histone, suggesting histonespecific protein methylase I.

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Energy Transfer between Calixarene and Naphthalene

  • Kook, Seong-Keun
    • Bulletin of the Korean Chemical Society
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    • v.23 no.8
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    • pp.1111-1115
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    • 2002
  • The photoluminescence of calixarene crystals has been studied as functions of temperature, time, and concentration. The vibronic bands shift to longer wavelength and become significantly sharper as temperature decreases. The experimental results r eveal that the structural transformation occur during the annealing process. Time-resolved spectra of calixarene at 12 K are monitored. Spectral features, which demonstrate characteristic of energy transfer processes, are not observed. The depopulation of excited state density is mainly controlled by unimolecular decay process dominating other decay processes. The lifetime was found to be 2.6 $\pm$ 0.1 ns. For the case of calixarene mixed with naphthalene, the fluorescence spectrum shows that the band centered at 340 nm lies 2840 $cm^{-1}$ below the relatively broad 310 nm band found for calixarene crystals. The spectra also exhibit that the emission intensity increases with increasing calixarene concentration. The results are evident that the calixarene emission is quenched by the naphthalene. Phosphorescence of calixarene mixed with naphthalene crystals is observed to determine whether the emission is due to naphthalene. The phosphorescence peaks were compared with the ground-state vibrational frequencies of naphthalene and found to be in good agreement. The results indicate that inter-molecular energy transfer occurs between calixarene and naphthalene.

Expression of Recombinant HBV Pol Proteins in HepG2 Cells

  • Cho, Ginam;Na, Seun-Gon;Suh, Se-Won;Jung, Gu-Hung
    • BMB Reports
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    • v.33 no.6
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    • pp.440-447
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    • 2000
  • In this study HepG2 cells were used to express and purify HBV pol proteins. In order to facilitate purification of HBV pol proteins, HBV pol and its deletion mutants were fused to MBP (Maltose Binding Protein). As a result we successfully expressed and partially purified both wild type and mutant recombinant HBV pol proteins by using an amylose resin and anti-MBP antibody. In the case of wild type, the anti-MBP antibody detected three bands. One was full-length and the others were generated by proteolysis of the terminal domain region. The expressed MBP/POL proteins were localized both in the cytoplasm and in the perinuclear region. The purified proteins had polymerase activity toward an exogenous homo-polymer template. The MBP/POL protein also had DNA synthesis activity in vivo, since the MBP/POL expression construct was able to complement a HBV polymerase mutant in trans.

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