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Characteristics of Sr2Ni1.8Mo0.2O6-δ Anode for Utilization in Methane Fuel Conditions in Solid Oxide Fuel Cells

  • Kim, Jun Ho;Yun, Jeong Woo
    • Journal of Electrochemical Science and Technology
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    • v.10 no.3
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    • pp.335-343
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    • 2019
  • In this study, $Sr_2Ni_{1.8}Mo_{0.2}O_{6-{\delta}}$ (SNM) with a double perovskite structure was investigated as an alternative anode for use in the $CH_4$ fuel in solid oxide fuel cells. SNM demonstrates a double perovskite phase over $600^{\circ}C$ and marginal crystallization at higher temperatures. The Ni nanoparticles were exsolved from the SNM anode during the fabrication process. As the SNM anode demonstrates poor electrochemical and electro-catalytic properties in the $H_2$ and $CH_4$ fuels, it was modified by applying a samarium-doped ceria (SDC) coating on its surface to improve the cell performance. As a result of this SDC modification, the cell performance improved from $39.4mW/cm^2$ to $117.7mW/cm^2$ in $H_2$ and from $15.9mW/cm^2$ to $66.6mW/cm^2$ in $CH_4$ at $850^{\circ}C$. The mixed ionic and electronic conductive property of the SDC provided electrochemical oxidation sites that are beyond the triple boundary phase sites in the SNM anode. In addition, the carbon deposition on the SDC thin layer was minimized due to the SDC's excellent oxygen ion conductivity.

Anti-atherosclerosis Effect of Imyosan Extract in Human Aortic Smooth Muscle Cells (사람 대동맥 평활근 세포에서 이묘산(二妙散)의 항동맥경화 활성)

  • Yun, Hyun-Jeong;Heo, Sook-Kyoung;Yi, Hyo-Seung;Kim, Tae-Hoon;Kim, Dong-Wan;Kim, Sun-Mo;Park, Sun-Dong
    • The Korea Journal of Herbology
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    • v.23 no.4
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    • pp.113-120
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    • 2008
  • Objectives: This study was evaluated to elucidate the inhibitory potential of Imyosan(IMS) and its components, Phellodendri Cortex(PC: Phellodendron amurense Rupr., Hwangbaek in Korean) and Atractylodis Rhizoma(AR: Atratylodes lancea D.C., Changchool in Korean), on human aortic smooth muscle cells(HASMC) migration and production of matrix metalloproteinase (MMP)-2 and MMP-9 by TNF-${\alpha}$ treatment. Methods: Cytotoxic activity of IMS and its components on HASMC was using 5-(3-caroboxy meth-oxyphenyl)-2H-tetra-zolium inner salt(MTS) assay. Effect of IMS, PC and AR on TNF-${\alpha}$-induced HASMC migration underside of matrigel filter was stained with hematoxylin-eosin. And total number of cells that migrated to the underside of the filter was counted. MMP-2 and MMP-9 activity was evaluated by gelatin zymography assay. Results: The matrigel migration assay showed that IMS effectively inhibited the TNF-${\alpha}$-induced migration of HASMC. Moreover, IMS significantly inhibited MMP-9 activity. Our present study demonstrates that IMS and its components inhibit TNF-${\alpha}$-induced HASMC migration and MMP-9 activity. The inhibitory effect of IMS extract is more potent than that of its component herb extracts. Conclusions: These results provide evidence that IMS has multiple effects in the inhibition of HASMC migration and may offer a therapeutic approach to block HASMC migration.

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Isolation and Characterization of an Agarase-Producing Bacterial Strain, Alteromonas sp. GNUM-1, from the West Sea, Korea

  • Kim, Jonghee;Hong, Soon-Kwang
    • Journal of Microbiology and Biotechnology
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    • v.22 no.12
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    • pp.1621-1628
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    • 2012
  • The agar-degrading bacterium GNUM-1 was isolated from the brown algal species Sargassum serratifolium, which was obtained from the West Sea of Korea, by using the selective artificial seawater agar plate. The cells were Gram-negative, $0.5-0.6{\mu}m$ wide and $2.0-2.5{\mu}m$ long curved rods with a single polar flagellum, forming nonpigmented, circular, smooth colonies. Cells grew at $20^{\circ}C-37^{\circ}C$, between pH 5.0 and 9.0, and at 1-10% (w/v) NaCl. The DNA G+C content of the GNUM-1 strain was 45.5 mol%. The 16S rRNA sequence of the GNUM-1 was very similar to those of Alteromonas stellipolaris LMG 21861 (99.86% sequence homology) and Alteromonas addita $R10SW13^T$(99.64% sequence homology), which led us to assign it to the genus Alteromonas. It showed positive activities for agarase, amylase, gelatinase, alkaline phosphatase, esterase (C8), lipase (C14), leucine arylamidase, valine arylamidase, ${\alpha}$-chymotrypsin, acid phosphatase, naphthol-AS-BI-phosphohydrolase, ${\alpha}$-galactosidase, ${\beta}$-galactosidase, ${\beta}$-glucosidase, catalase, and urease. It can utilize citrate, malic acid, and trisodium citrate. The major fatty acids were summed feature 3 (21.5%, comprising $C_{16:1}{\omega}7c/iso-C_{15:0}$ 2-OH) and C16:0 (15.04%). On the basis of the variations in many biochemical characteristics, GNUM-1 was considered as unique and thus was named Alteromonas sp. GNUM-1. It produced the highest agarase activity in modified ASW medium containing 0.4% sucrose, but lower activity in rich media despite superior growth, implying that agarase production is tightly regulated and repressed in a rich nutrient condition. The 30 kDa protein with agarase activity was identified by zymography, and this report serves as the very first account of such a protein in the genus Alteromonas.

The study on water quality and phytoplankton flora at 3 rivers in the Taejon city (대전시 3대 하천의 수질 및 식물플랑크톤상에 관한 연구)

  • 강창민;이상명;엄준식;이정희;이호원;홍춘표
    • Journal of Environmental Science International
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    • v.9 no.4
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    • pp.275-284
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    • 2000
  • The studyies on physico-chemical factors and phytoplankton at the 3 rivers in the Taejon city were conducted from November 1997 to May 1998. The Results were as floows; In the water quality, the down streams were generally worse than the upper streams. Water temperature was varied from 2.4$^{\circ}C$ to 23.$0^{\circ}C$; DO from 1.80mg/$\ell$ to 17.6mg/$\ell$ ; pH from 4.7 to 10.4 ; BOD from 0.78mg/$\ell$ to 8.80mg/$\ell$ ; COD from 0.32mg/$\ell$ to 8.26mg/$\ell$ ; SS from 2.0mg/$\ell$ to 43.0mg/$\ell$ ; total phosphate was from 0.001mg/$\ell$ to 0.709mg/$\ell$ ; total nitrogen 0.01mg/$\ell$ to 11.69mg/$\ell$. In phytoplankton species, they were identified as total 191 taxa composed of 8 classes, 18 orders, 35 families, 74 genera, 152 species, 35 varieties and 4 forms. The dominant species were Synedra ulna in Taejon-chon, Diatomavulgare in Yudong-chon, Oscillatioria princeps, Scenedesmus qadricauda, Synedra ulna, and Diatom vulgare in Gap-chon. Standing crops of phytoplankton were from 2,076 cells/$m\ell$ to 97,356 cells/$m\ell$

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Effects of Co-culture with Uterine or Oviductal Epitherial Cells on Development of Korean Native Cattle Oocytes Fertilized In Vitro (한우 체외수정란의 발달에 자궁상피세포 및 난관 상피세포의 공배양이 미치는 영향)

  • 최선호;양병철;김일화;손동수;이광원;이동원
    • Journal of Embryo Transfer
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    • v.11 no.1
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    • pp.7-14
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    • 1996
  • The object of this study was to evaluate the effect of uterine epithelial cells on development of Korean native cattle(KNC) oocytes fertilized in vitro. Qocytes were collected from ovaries of slaughtered Korean Native Cows and matured in TCM199 with granulosa cells supplemented with 10% FBS, 5$\mu$g/ml FSH, 10 JU/ml hCG, and 1$\mu$g/ml estradiol-17$\beta$ for 24 hrs. For co-culture of in vitro development of fertilized ova, oviductal epithelial cells (l$\times$l0˚cells /ml) obtained from slaughtered cow and uterine epithelial cells(1$\times$10˚cells /ml) flushed from the superovulated holstein on Day 7 were incubated in 39$^{\circ}C$, 5% $CO_2$, 95% air. Frozen-thawed KNC sperm was capacitated with BO(Brackett & Oliphant, 1975) medium supplemented with 10mM, 5mM-caffein. Matured oocytes were inseminated for 20 hrs. And then fertilized oocytes were washed with culture medium and transferred to oviductal epithelial cells for in vitro development and three days later a portion of embryos were transferred to uterine epithelial cells. Stastical methods of developmental rates on KNC-IVF oocytes was ANOVA-test. Developmental rates of KNC-IVF oocytes was significant higher(P<0.01) when co-cul-tured with uterine epithelial cells(25.2%) than oviductal epithelial cells. Blatocyst cul-tured for 7 to 9 days were frozen by automatic freezer with 1.4M glycerol-PBS. Survival rates of blastocyst was 40.0%. Fourteen frozen-thawed blastocysts were transferred to five holstein heifers on day 7 after natural estrus. Three recipients were observed twin and one recipient was single by ultra-sound systems on days 45 after embryo transfer.

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Purification and Characterization of Two Extracellular Proteases from Oligotropha carboxydovorans DSM 1227

  • Kang, Beom-Sik;Jeon, Sang-Jun;Kim, Young-Min
    • Journal of Microbiology
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    • v.37 no.1
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    • pp.14-20
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    • 1999
  • Two extracellular proteases, EP I and EP II, from cells of Oligotropha carboxydovorans (formerly Pseudomonas carboxydovorans) DSM 1227 grown in nutrient broth were purified to greater than 95% homogeneity in five steps using azocasein as a substrate. The final specific activities of EPs I and II were 214.9 and 667.4 units per mg of protein. The molecular weights of native EPs I and II were determined to be 23,000. Sodium dodecyl sulfate-gel electrophoresis revealed the two enzymes to be monomers. The enzymes were found to be serine-type proteases. The activity of EP I was stimulated by Ca2+, Mg2+, and Ba2+, but that of EP II was not. The enzymes were completely inhibited by Fe2+, Hg2+, Co2+, Zn2+, and Cd2+. EDTA and EGTA exhibited a strong inhibitory effect on EP I. The optimal pH for the two enzymes was pH 9.0. The optimal temperatures for EP I and II were 60 and 50$^{\circ}C$, respectively. The enzymes were stable under alkaline conditions. The thermal stability of EP I was higher than that of EP II. Cell-free extracts did not inhibit the purified enzymes. The enzymes were active on casein, azocasein, azocoll, and carbon monoxide dehydrogenase, but weakly active with bovine serum albumin.

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A Novel Metalloprotease from the Wild Basidiomycete Mushroom Lepista nuda

  • Wu, Y.Y.;Wang, H.X.;Ng, T.B.
    • Journal of Microbiology and Biotechnology
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    • v.21 no.3
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    • pp.256-262
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    • 2011
  • A 20.9-kDa metalloprotease was isolated from dried fruiting bodies of the wild basidiomycete mushroom Lepista nuda. The N-terminal amino acid sequence of the protease was seen to be ATFVLTAATNTLFTA, thus displaying no similarity with the sequences of previously reported metalloproteases. The protease was purified using a procedure that entailed ion-exchange chromatography on CM-Cellulose, Q-Sepharose, and Mono S, and FPLC-gel filtration on Superdex 75. The protease functioned at an optimum pH of 7.0 and an optimum temperature of $50^{\circ}C$. It was also noted that the protease demonstrated a proteolytic activity of 1,756 U/mg toward casein. The $K_m$ of the purified protease toward casein was 6.36 mg/ml at a pH of 7.0 and with a temperature of $37^{\circ}C$, whereas the $V_{max}$ was 9.11 ${\mu}g\;ml^{-1}\;min^{-1}$. The activity of the protease was adversely affected by EDTA-2Na, suggesting that it is a metalloprotease. PMSF, EGTA, aprotinin, and leupeptin exerted no striking inhibitory effect. The activity of the protease was enhanced by $Fe^{2+}$, but was curtailed by $Cd^{2+}$, $Cu^{2+}$, $Hg^{2+}$, $Pb^{2+}$, $Zn^{2+}$, and $Fe^{2+}$ ions. The protease also exhibited inhibitory activity against HIV-1 reverse transcriptase with an $IC_{50}$ value of 4.00 ${\mu}M$. The $IC_{50}$ values toward hepatoma Hep G2 and leukemia L1210 cells in vitro were 4.99 ${\mu}M$ and 3.67 ${\mu}M$, respectively.

Anti-proliferative Effects by Aqueous Extract of Cordyceps Militaris in Human Leukemic U937 Cells (동충하초 추출물에 의한 U937 인체 백혈병 세포의 성장억제 효과)

  • Park, Dong-Il;Seo, Sang-Ho;Choi, Yung-Hyun;Hong, Sang-Hoon
    • Journal of Physiology & Pathology in Korean Medicine
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    • v.19 no.2
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    • pp.452-458
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    • 2005
  • Cordyceps militaris is a medicinal fungus, which has been used for patient suffering from cancer in Oriental medicine. It was reported previously that C. militaris extracts are capable of inhibiting tumor growth, however, the anti-poliferative effects of human cancer cells have not been poorly understood. In this study, to elucidate the growth inhibitory mechanisms of human cancer cells by treatment of aqueous extract of C. militaris (AECM) we investigated the anti-proliferative effects of AECM in human leukemia U937 cell line. AECM treatment inhibited the growth of U937 cells and induced the apoptotic cell death in a concentration-dependent manner, which was associated with morphological changes. We observed the up-regulation of cyclin-dependent kinase (Cdk) inhibitor p21(WAF1/CIP1) by p53-independent manner and activation of caspase-3 in AECM-treated U937 cells, however, the activity of caspase-9 was remained unchanged. Additionally, AECM treatment caused a dose-dependent inhibition of the expression of telomere regulatory gene products such as human telomere reverse transcriptase (hTERT) and telomerase-associated protein-1 (TEP-1). Taken together, these findings suggest that AECM-induced inhibition of human leukemic cell proliferation is associated with the induction of apoptotic cell death via modulation of several major growth regulatory gene products, and C. militaris may have therapeutic potential in human lung cancer.

Physiological Effect of Yogurt with Powder Two Stage Fermented Dioscorea batatas Dence by Monascus sp. and Lactobacillus sp. (Monascus sp.와 Lactobacillus sp.를 이용한 2단 발효마 분말 첨가 요구르트의 생리활성 효과)

  • Jeon, Chun-Pyo;Lee, Jung-Bok;Choi, Chung-Sig;Kwon, Gi-Seok
    • Korean Journal of Microbiology
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    • v.47 no.2
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    • pp.151-157
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    • 2011
  • This study was to examine the quality characteristics and biological activities of the yogurt containing dual fermentation MFCY (Monascus-Fermented Chinese Yam) powder. Six different contents (0, 0.1, 0.3, 0.5, 1.0, and 2.0%, w/v) of MFCY powder were added to raw milk and 5% skim milk followed by fermentation with lactic acid bacteria at $37^{\circ}C$ for 12 h, and then the biological activities of the samples were investigated. Biological activities of the prepared yogurt were evaluated for acid production (pH, titratable acidity), number of viable cells, total polyphenol contents, DPPH radical scavenging activity, reducing power, angiotensin converting enzyme inhibitory effects and GABA contents. In this study, the results show that after fermentation in raw milk and 5% skim milk added with MFCY powder. The yogurt can produced pH, titratable acidity, number of viable cells, total polyphenol contents, DPPH radical scavenging activity and reducing power at 4.12-4.25 (pH), 0.94-0.97% (TA), $7.50{\times}10^9-1.14{\times}10^{10}$ CFU/ml, 161.4-329.9 (TP, mg/L), 54-94% (DPPH), and 1.13-1.53 (R.P), respectively. In addition, the showed ACE inhibitory activity and GABA contents was 67.1-87.7% and 304.6-685.4 (mg/L).

Oxidative Stress-dependent Structural and Functional Regulation of 2-cysteine Peroxiredoxins In Eukaryotes Including Plant Cells (산화 스트레스에 의존한 식물 및 진핵세포 2-시스테인 퍼록시레독신의 기능 조절)

  • Jang, Ho-Hee;Kim, Sun-Young;Lee, Sang-Yeol
    • Journal of Plant Biotechnology
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    • v.33 no.1
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    • pp.1-9
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    • 2006
  • Peroxiredoxins (Prxs) are ubiquitously distributed and play important functions in diverse cellular signaling systems. The proteins are largely classified into three groups, such as typical 2-Cys Prx, atypical 2-Cys Prx, and 1-Cys Prx, that are distinguished by their catalytic mechanisms and number of Cys residues. From the three classes of Prxs, the typical 2-Cys Prx containing the two-conserved Cys residues at its N-terminus and C-terminus catalyzes $H_2O_2$ with the use of thioredoxin (Trx) as an electron donor. During the catalytic cycle, the N-terminal Cys residue undergoes a peroxide-dependent oxidation to sulfenic acid, which can be further oxidized to sulfinic acid at the presence of high concentrations of $H_2O_2$ and a Trx system containing Trx, Trx reductase, and NADPH. The sulfinic acid form of 2-Cys Prx is reduced by the action of sulfiredoxin which requires ATP as an energy source. Under the strong oxidative or heat shock stress conditions, 2-Cys Prx in eukaryotes rapidly switches its protein structure from low-molecular-weight species to high-molecular-weight protein structures. In accordance with its structural changes, the protein concomitantly triggers functional switching from a peroxidase to a molecular chaperone, which can protect its substrate denaturation from external stress. In addition to its N-terminal active site, the C-terminal domain including 'YF-motif' of 2-Cys Prx plays a critical role in the structural changes. Therefore, the C-terminal truncated 2-Cys Prxs are not able to regulate their protein structures and highly resistant to $H_2O_2$-dependent hyperoxidation, suggesting that the reaction is guided by the peroxidatic Cys residue. Based on the results, it may be concluded that the peroxidatic Cys of 2-Cys Prx acts as an '$H_2O_2$-sensor' in the cells. The oxidative stress-dependent regulation of 2-Cys Prx provides a means of defense systems in cells to adapt stress conditions by activating intracellular defense signaling pathways. Particularly, 2-Cys Prxs in plants are localized in chloroplasts with a dynamic protein structure. The protein undergoes conformational changes again oxidative stress. Depending on a redox-potential of the chloroplasts, the plant 2-Cys Prx forms super-molecular weight protein structures, which attach to the thylakoid membranes in a reversible manner.