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      • 난관배양액이 처녀발생유기된 돼지난포란의 체외발달에 미치는 영향

        문승주,이경호,김호,김창렬,은대숙,김광현,나진수,김재홍 全南大學校 農業科學技術硏究所 1997 農業科學技術硏究 Vol.32 No.-

        본 연구는 난관배양액이 돼지수정란의 체외발달에 미치는 효과를 규명키 위하여 수행하였다. 돼지 미성숙 난포란은 TCM-199, Ham's F-10 그리고 Whitten's 배양액에 10% 난포액과 호르몬(PMSG : 10IU/㎖, HCG : 10IU/㎖)을 첨가 20시간 배양하고 호르몬을 첨가하지 않는 배양액에서 20시간 추가 배양하여 총 40시간동안 배양하여 체외성숙을 유도하였다. 체외성숙후 0.1% hyaluronidase로 난구세포를 제거하고 15% FCS가 함유된 TCM-199으로 3회 세척하고 TCM-199에 15% FCS와 10% ethanol 혼합액에 세척한 난자를 옮겨 10분간 배양 처녀발생을 유기하였다. 처녀발생 6시간후 전핵형성율은 체외성숙배양액으로 TCM-199을 사용했을 때 56.4%, Ham's F-10의 경우 58.3%, Whitten's 배양액의 경우 74.0%를 보였다. 처녀발생 유기 48시간째 난할율은 TCM-199을 사용했을 때 45.7%, Ham's F-10에서 45.4%, Whitten's배양액에서 39.2%를 보였으며 세종류의 배양액에 POCM을 첨가 배양했을 때 TCM-199에 44.8%, Ham's F-10에서 45.4%, Whitten's배양액에서 43.7%로 나타났다. 처녀발생육 난자를 96시간 체외배양시킨 결과 상실배 발달율이 POCM을 첨가 했을 때 첨가하지 않은 시험구에 비하여 유의적으로 높았다(P<0.05) The effect of porcine oviductal conditioned medium(POCM) on in vitro development of chemically activated porcine oocytes was studied. Porcine oocytes were cultured in TCM-199, Ham's F-10 and Whitten's medium with hormonal supplements for 20h and 40h additional culture without hormonal supplements. After in vitro maturation, the denuded oocytes were washed 3 times with TCM-199 contaning 15%(v/v) ethanol to induce pathenogenetic activation. At 6h after activation, pronuclea formation rates were 56.4% in TCM-199, 59.3% in Ham's F-10 and 74.0% in Whitten's maturation medium. At 48h after activation, 45.7%, 45.4% and 39.2% of oocytes claved in TCM-199, Ham's F-10 and Whitten's culture medium, respectively. And 44.8%, 45.5% and 43.7% of oocytes were claved in TCM-199, Ham;s F-10 and Whitten's culture medium supplemented with POCM, respectively. The rates of moular were higher in culture medium with POCM than without POCM at 96h after activation.(P<0.05)

      • KCI등재
      • Biochemical Properties of a Novel Cysteine Protease of <i>Plasmodium vivax</i> , Vivapain-4

        Na, Byoung-Kuk,Bae, Young-An,Zo, Young-Gun,Choe, Youngchool,Kim, Seon-Hee,Desai, Prashant V.,Avery, Mitchell A.,Craik, Charles S.,Kim, Tong-Soo,Rosenthal, Philip J.,Kong, Yoon Public Library of Science 2010 PLoS neglected tropical diseases Vol.4 No.10

        <▼1><P><B>Background</B></P><P>Multiple cysteine proteases of malaria parasites are required for maintenance of parasite metabolic homeostasis and egress from the host erythrocyte. In <I>Plasmodium falciparum</I> these proteases appear to mediate the processing of hemoglobin and aspartic proteases (plasmepsins) in the acidic food vacuole and the hydrolysis of erythrocyte structural proteins at neutral pH. Two cysteine proteases, vivapain (VX)-2 and VX-3 have been characterized in <I>P. vivax</I>, but comprehensive studies of <I>P. vivax</I> cysteine proteases remain elusive.</P><P><B>Findings</B></P><P>We characterized a novel cysteine protease of <I>P. vivax</I>, VX-4, of which orthologs appears to have evolved differentially in primate plasmodia with strong cladistic affinity toward those of rodent <I>Plasmodium</I>. Recombinant VX-4 demonstrated dual substrate specificity depending on the surrounding micro-environmental pH. Its hydrolyzing activity against benzyloxycarbonyl-Leu-Arg-4-methyl-coumaryl-7-amide (Z-Leu-Arg-MCA) and Z-Phe-Arg-MCA was highest at acidic pH (5.5), whereas that against Z-Arg-Arg-MCA was maximal at neutral pH (6.5–7.5). VX-4 preferred positively charged amino acids and Gln at the P1 position, with less strict specificity at P3 and P4. P2 preferences depended on pH (Leu at pH 5.5 and Arg at pH 7.5). Three amino acids that delineate the S2 pocket were substituted in VX-4 compared to VX-2 and VX-3 (Ala90, Gly157 and Glu180). Replacement of Glu180 abolished activity against Z-Arg-Arg-MCA at neutral pH, indicating the importance of this amino acid in the pH-dependent substrate preference. VX-4 was localized in the food vacuoles and cytoplasm of the erythrocytic stage of <I>P. vivax</I>. VX-4 showed maximal activity against actin at neutral pH, and that against <I>P. vivax</I> plasmepsin 4 and hemoglobin was detected at neutral/acidic and acidic pH, respectively.</P><P><B>Conclusion</B></P><P>VX-4 demonstrates pH-dependent substrate switching, which might offer an efficient mechanism for the specific cleavage of different substrates in different intracellular environments. VX-4 might function as a hemoglobinase in the acidic parasite food vacuole, a maturase of <I>P. vivax</I> plasmepsin 4 at neutral or acidic pH, and a cytoskeleton-degrading protease in the neutral erythrocyte cytosol.</P></▼1><▼2><P><B>Author Summary</B></P><P><I>Plasmodium vivax</I> affects hundreds of millions each year and results in severe morbidity and mortality. Plasmodial cysteine proteases (CPs) play crucial roles during the progression of malaria since inhibition of these molecules impairs parasite growth. These CPs might be targeted for new antimalarial drugs. We characterized a novel <I>P. vivax</I> CP, vivapain-4 (VX-4), which appeared to evolve differentially among primate <I>Plasmodium</I> species. VX-4 showed highly unique substrate preference depending on surrounding micro-environmental pH. It effectively hydrolyzed benzyloxycarbonyl-Leu-Arg-4-methyl-coumaryl-7-amide (Z-Leu-Arg-MCA) and Z-Phe-Arg-MCA at acidic pH and Z-Arg-Arg-MCA at neutral pH. Three amino acids (Ala90, Gly157 and Glu180) that delineate the S2 pocket were found to be substituted in VX-4. Alteration of Glu180 abolished hydrolytic activity against Z-Arg-Arg-MCA at neutral pH, indicating Glu180 is intimately involved in the pH-dependent substrate preference. VX-4 hydrolyzed actin at neutral pH and hemoglobin at acidic pH, and participated in plasmepsin 4 activation at neutral/acidic pH. VX-4 was localized in the food vacuoles and cytoplasm of the erythrocytic stage of <I>P. vivax</I>. The differential substrate preferences depending on pH suggested a highly efficient mechanism to enlarge biological implications of VX-4, including hemoglobin degradation, maturation of plasmepsin, and remodeling of the parasite architecture during growth and development of <I>P. vivax</I>.</P></▼2>

      • KCI등재후보

        살모넬라의 Fimbrial Adhesion Group에 포함되는 Type 1 Fimbriae 유전자 분석

        나훈택 ( Hun-taek Na ),정맹식 ( Maeng Sig Joung ),김홍선 ( Hong S. Kim ),이시경 ( Si Kyung Lee ),홍지애 ( J. A. Hong ),김수영 ( Soo Young Kim ) 한국자연치유학회 2017 Journal of Naturopathy Vol.6 No.1-2

        본 연구에서는 살모넬라 표준균주 4종과 분리균주 2종을 대상으로 type 1 fimbriae 유전자 fimC, fimD, fimI, fimZ를 각각 비교한 결과 많은 아미노산 변이가 관찰되었다. S. typhimurium ATCC 14028 균주에서 가장 많은 14개의 아미노산 변이가 관찰되었다. 반면 S. typhimurium ATCC 13311 균주에서는 가장 적은 2개의 아미노산 변이가 관찰되었다. 그중에서 유전자 fimC와 fimZ에서는 아미노산 변이가 관찰되지 않았고, fimD와 fimI 유전자에서 Leu527→Pro, Ile130→Val으로 각각 아미노산 변이가 관찰되었다. In this study, a number of amino acid mutations were observed in the type 1 fimbriae genes fimC, fimD, fimI, and fimZ in four Salmonella reference strains and two isolates. S. typhimurium ATCC 14028 strain showed most numerous 14 amino acid variations. On the other hand S. typhimurium ATCC 13311 strain, the least two amino acid variants were observed. Among them, amino acid mutations were not observed in the genes fimC and fimZ, and in the fimD and fimI genes, amino acid variations were observed as Leu527→Pro, Ile130→Val.

      • SCISCIESCOPUS

        Fluorescent chemosensor based-on the combination of julolidine and furan for selective detection of zinc ion

        Na, Y.J.,Hwang, I.H.,Jo, H.Y.,Lee, S.A.,Park, G.J.,Kim, C. Elsevier 2013 Inorganic Chemistry Communications Vol.35 No.-

        A new sensor 1-[[(2-furanylmethyl)imino]methyl]-2-hydroxyjulolidine (1) based on the combination of julolidine and furan groups was designed and synthesized as a Zn<SUP>2+</SUP> selective fluorescent chemosensor. Upon treatment with zinc ions, the complexation of 1 with Zn<SUP>2+</SUP> exhibited a pronounced enhancement in the fluorescence emission in methanol, while many other ions such as Mn<SUP>2+</SUP>, Co<SUP>2+</SUP>, Ni<SUP>2+</SUP>, Cd<SUP>2+</SUP>, Hg<SUP>2+</SUP>, Na<SUP>+</SUP>, K<SUP>+</SUP>, Mg<SUP>2+</SUP>, Ca<SUP>2+</SUP>, Al<SUP>3+</SUP> and Ag<SUP>+</SUP>, had no influence. Notably, this chemosensor could distinguish clearly Zn<SUP>2+</SUP> from Cd<SUP>2+</SUP>. The 1:1 binding mode of the 1-Zn<SUP>2+</SUP> complex was drawn, based on UV-vis titration, fluorescence titration, Job plot and ESI-mass spectrometry analysis.

      • 조직구성 수성 망상증 1예

        나한식,조경상,김종두,이승일,문철웅,이호영,장숙진 朝鮮大學校 附設 醫學硏究所 1989 The Medical Journal of Chosun University Vol.14 No.2

        Histiocytic medullary reticulosis is a clinicopathologic syndrome characterized by its acute onset and relentless progression to death within a few months. The major clinical features are fever, malaise, weakness, weight loss, lymphadenopathy, hepatosplenomegaly, jaundice and purpura. The common laboratory findings are severe anemia, leukopenia, and thrombocytopenia. Histologically, bone marrow were infiltrated with atypical, neoplastic histiocytes, many of which had ingested large number of red blood cells, leukocyte, platelet. We experienced one case of HMR who was a 22 year old male admitted via ER with malaise, general weakness, fever and headache. The patient died often 11 days of illness. Death was due to massive bleeding and DIC thought to be due to pancytopenia secondary to massive blood element phagocytosis. So, we reported one case which considered compatible for HMR, with a few elementary reviewed literatures.

      • KCI등재

        α - 셀룰로오즈의 열분해에 관한 연구 : 산촉매 NaCl 의 영향 Effect of Acid Catalsts NaCl

        나상도,황준호,최경선,설수덕,손진언 한국고무학회 1996 엘라스토머 및 콤포지트 Vol.31 No.2

        The Thermal decomposition of the α-Cellulose and NaCl was studied using a thermal analysis technique in the steam of nitrogen gas with 30㎖/min at various heating ranges from 4 to 20℃/min. The Derivative and Integral method used to be obtained values of activation energy of decomposition reaction. 1. The values of activation energy evaluated by Derivative and Intergral method were consistent with each other very well. 2. The maximum value of heat of decomposition evalated by DSC method was α-Cellulose/NaCl=90/10. 3. The thermogravimetric trace curve agreed with the theoretical equation.

      • SCIESCOPUSKCI등재

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