• Microbiology and Biotechnology Letters
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• v.14 no.2
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• pp.169-174
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• 1986

Cytosine deaminase was partialy purified about 10 fold from the ceil-free extract of Aspergillus fumigatus. The partialy purified enzyme was relatively stable in a pH 5.5 to 8.0, but thermo-unstable. The enzyme activity was found in a pH optimum of 7.0 and temperature optimum of 30 to 35$^{\circ}C$. The activation energy calculated to be 13,240 cal/mol. The apparent Michaelis constants Km for cytosine was found to be 1.53 mM and the molecular weight was determined to be approximately 32,000. The enzyme was strongly inhibited by 0.1 mM of Hg$^^{2+}$, Pb$^{2+}$, Cd$^{2+}$ and Fe$^{2+}$, furthermore inhibited by 1mM of ATP, UTP, o-phenanthroline and p-chloromercuribenzoate.

• The Korean Journal of Mycology
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• v.32 no.2
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• pp.119-124
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• 2004

Metalloenzyme was purified from the fruiting bodies of Tricholoma sejunctum. MALDI-TOF and ICP/MS analyses revealed that the enzyme had a molecular weight of 18788.25 and includes $Zn^{2+}$ ion. The N-terminal amino acid sequence of the enzyme was Ala-Thr-Tyr-Lys-Ile-X-Ser-Ala-Thr-His-Gln-X-X-Leu-Val. The activity of the enzyme was inhibited by EDTA and 1,10-phenanthroline, indicating that the enzyme was a metalloprotease. No inhibition was found with E-64 and pepstatin. It has broad substrate specificity for synthetic peptides. The enzyme was stable up to $40^{\circ}C$. The activity of the enzyme was increased by $Zn^{2+}$ and $Co^{2+}$, while it was totally inhibited by $Hg^{2+}$. The enzyme hydrolyzes $A{\alpha}$ subunit of human fibrinogen but did not show any reactivity for $B{\beta}$ and ${\gamma}$ form of human fibrinogen.

• Parasites, Hosts and Diseases
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• v.52 no.6
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• pp.595-603
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• 2014

Trichomonas vaginalis secretes a number of proteases which are suspected to be the cause of pathogenesis; however, little is understood how they manipulate host cells. The mammalian target of rapamycin (mTOR) regulates cell growth, cell proliferation, cell motility, cell survival, protein synthesis, and transcription. We detected various types of metalloproteinases including GP63 protein from T. vaginalis trophozoites, and T. vaginalis GP63 metalloproteinase was confirmed by sequencing and western blot. When SiHa cells were stimulated with live T. vaginalis, T. vaginalis excretory-secretory products (ESP) or T. vaginalis lysate, live T. vaginalis and T. vaginalis ESP induced the mTOR cleavage in both time-and parasite load-dependent manner, but T. vaginalis lysate did not. Pretreatment of T. vaginalis with a metalloproteinase inhibitor, 1,10-phenanthroline, completely disappeared the mTOR cleavage in SiHa cells. Collectively, T. vaginalis metallopeptidase induces host cell mTOR cleavage, which may be related to survival of the parasite.

• Journal of the Korean Chemical Society
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• v.57 no.6
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• pp.703-711
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• 2013

In the present investigation, kinetic studies of oxidation of formic acid with and without catalyst and promoter in aqueous acid media were studied under the pseudo-first order conditions [formic acid]T ${\gg}[Cr(VI)]_T$ at room temperature. In the 1,10-phenanthroline (phen) promoted path, the cationic Cr(VI) phen complex is the main active oxidant species undergoes a nucleophilic attack by the substrate to form a ternary complex which subsequently experiences a redox decomposition through several steps leading to the products $CO_2$ and $H_2$ along with the Cr(III) phen complex. The anionic surfactant (i.e., sodium dodecyl sulfate, SDS) and neutral surfactant (i.e., Triton X-100, TX-100) act as catalyst and the reaction undergo simultaneously in both aqueous and micellar phase with an enhanced rate of oxidation in the micellar phase. Whereas the cationic surfactant (i.e., N-cetyl pyridinium chloride, CPC) acts as an inhibitor restricts the reaction to aqueous phase. The observed net enhancement of rate effects has been explained by considering the hydrophobic and electrostatic interaction between the surfactants and reactants. The neutral surfactant TX-100 has been observed as the suitable micellar catalyst for the phen promoted chromic acid oxidation of formic acid.

• Microbiology and Biotechnology Letters
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• v.26 no.5
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• pp.420-426
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• 1998

An extracellular glutamyl aminopeptidase (EC 3.4.11.7) producing bacterium was isolated from soil and identified as Bacillus licheniformis based on its morphological and physiological characteristics. The aminopeptidase was purified to homogeneity by ammonium sulfate precipitation, Phenyl Sepharose, Resource Q, and Superose 12 column chromatographies. The specific activity of the purified aminopeptidase was 9.2 unit/mg for glutamyl p-nitroanilide with 17.6 purification folds. The purified aminopeptidase had an estimated molecular mass of 64 kDa consists of two different subunits (42 kDa and 22 kDa), and its isoeletric point was 5.2 measured by isoelectric focusing. The optimum pH and temperature of the aminopeptidase were 8.0 and 55$^{\circ}C$, respectively. The aminopeptidase was inhibited by EDTA and 1,10-phenanthroline, suggesting it be a metalloenzyme. Comparing with other aminopeptidase, the enzyme showed relatively high activity against peptide having glutamic acid as N-terminal.

• Biomedical Science Letters
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• v.6 no.4
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• pp.261-268
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• 2000

Fibrinolytic enzyme (FE-2) was purified from the fruiting bodies of Tricholoma saponaceum using DEAE-Cellulose chromatography and Mono-S column chromatography, The enzyme has a molecular weight of 18.23 kDa and include Zn$^{2+}$ ion as found by ICP/MS. The N-terminal amino acid sequence of the enzyme was A-L-Y-V-G-X-S-P-X-Q-Q-S-L-L-V It has a pH optimum at pH 7.5, suggested that FE-2 was a neutral pretense. The activity of FE-2 was highly inhibited by EDTA and 1,10-phenanthroline, indicating that the enzyme is a metalloprotease. The activity of FE-2 was increased by $Mg^{2+}$, Zn$^{2+}$, Fe$^{2+}$, and Co$^{2+}$, but the enzyme activity was totally inhibited by Hg$^{2+}$. No inhibition was found with PMSF, E-64, pepstatin and 2-mercaptoethanol. The enzyme hydrolyzed both $A\alpha$ and B$\beta$ chains of human fibrinogen. The $\gamma$ chain was resistant to hydrolysis by FE-2.

• Proceedings of the Korean Vacuum Society Conference
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• 2011.02a
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• pp.270-270
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• 2011

유기발광소자는 자발광소자의 강점들과 낮은 구동 전압으로 발광효율이 높아 디스플레이 소자와 백색 조명 광원으로 응용 가능성 때문에 발광효율 증진에 대한 연구가 활발히 진행되고 있다. 유기물 내에서의 정공의 이동도가 전자의 이동도보다 높아 발광층에서 정공과 전자의 수의 불균형이 나타나 재결합율이 떨어져 발광효율이 낮아지는 문제점이 있다. 본 연구에서는 전자의 이동도의 향상을 통한 발광층에서의 정공과 전자 재결합 효율을 향상하기 위해 전자수송층과 발광층으로 사용되는 tris(8-hydroxyquinolate)aluminum (Alq3)층에 Alq3보다 높은 전자이동도를 가지는 7-diphenyl-1,10-phenanthroline (BPhen)을 전자 수송층에 도핑하여 유기발광소자를 제작하였다. 2,9-dimethyl-4,7-diphenyl-1,10-phenanthroline을 정공저지층으로 사용하여 제작된 단일전자 소자를 이용하여 BPhen이 도핑된 전자 수송층을 사용한 소자가 Alq3만을 전자 수송층으로 사용한 소자보다 같은 전압에서 더 높은 전류밀도를 나타내었다. 전류밀도-전압특성 측정으로 전하 수송 메카니즘을 관찰하였다. 두 가지 전자 수송층을 사용하여 발광 소자를 제작하여 발광세기와 발광효율을 측정한 결과 도핑 된 전자 수송층을 사용하여 제작된 발광소자에서 발광세기와 발광효율이 향상되었다. 발광세기와 발광효율이 향상된 원인은 도핑된 전자수송층에서 높아진 전자의 이동도로 인하여 발광층에서 정공과 전자의 이동도가 균형을 이루어 전자-정공의 재결합 확률이 증가하기 때문이다. 도핑 된 전자 수송층을 사용하여 제작된 유기발광소자의 발광효율 향상에 대한 원인을 실험결과를 사용하여 설명 할 것이다.

• Applied Biological Chemistry
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• v.41 no.5
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• pp.349-354
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• 1998

The protease produced by Bacillus subtilis YG-95 was purified by precipitating with ammonium sulfate, DEAE-sepharose 6B and Sephadex G-100 column chromatogtaphies and its purified enzymological characteritics were investigated. The molecular weight of purified protease was estimated about 43kilodalton by SDS PAGE The optimum pH and temperature for the purified protease activity were pH 10.0 and $55^{\circ}C$, respectively. The enzyme was stable in broad range of pH 5.0 to 12.0. and at the below $45^{\circ}C$. The purified enzyme activty was inhibited by $Fe^{3+}$ and $Al^{3+}$. The activity was significantly inhibited more than 80% by O-Phenanthroline, PMSF and SDS. The $K_m$ value of the purified enzyme against Soy Protein Isolate as a substrate was 1.28 mg/ml.

• Applied Science and Convergence Technology
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• v.24 no.6
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• pp.278-283
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• 2015

In this work, the electrical bistability of an organic CT complex is demonstrated and the possible switching mechanism is proposed. 2,9-Dimethyl-4,7-diphenyl-1,10-phenanthroline (BCP) and tetracyanoquinodimethane (TCNQ) are used as an organic donor and acceptor, respectively, and poly-methamethylacrylate (PMMA) is used as a polymeric matrix for spin-coating. A device with the Al/($Al_2O_3$)/PMMA:BCP:TCNQ[1:1:0.5 wt%]/Al configuration demonstrated bistable and switching characteristics similar to Ovshinsky switching with a low threshold voltage and a high ON/OFF ratio. An analysis of the current-voltage curves of the device suggested that electrical switching took place due to the charge transfer mechanism.

• Journal of the Korean Institute of Electrical and Electronic Material Engineers
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• v.24 no.8
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• pp.678-681
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• 2011

We have investigated the effect of organic thin film on the driving voltage of OLED (organic light emitting diode) by inserting a 5 nm thick 2,9-dimethyl-4,7-diphenyl-1,10-phenanthroline (BCP) or triphenylphosphineoxide ($Ph_3PO$) between tris-(8-hydroxyquinoline)aluminum ($Alq_3$) electron transport layer and 4,4'-bis(2,2'-diphyenylvinyl)-1,1'-biphenyl (DPVBi) emission layer. The device with 5 nm thick $Ph_3PO$ layer exhibited higher maximum current efficiency and lower driving voltage than the device with BCP layer, resulting from better electron injection from $Alq_3$ to DPVBi in the device with $Ph_3PO$ layer.