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해양동물 렉틴 ( 제 11 보 ) : 조각매물고둥 렉틴의 림프구 분열효과 및 면역화학적 특성
전경희,서영아,소명숙,정시련 ( Kyung Hee Jeune,Young Ah Suh,Myung Suk So,See Ryun Chung ) 생화학분자생물학회 1991 BMB Reports Vol.24 No.3
Developing new substances for immunosuppressor or immunomodulator from natural products is extremely important in the present biomedicine. In this paper, we focused our efforts on the mitogenicity and immunochemical properties of the NI lectins (NIA, NIB, NIC), obtained from Neptunea intersculpta. Immunochemical techniques were employed to elucidate the structural and/or functional similarities between the NI lectins. According to these results, NIB and NIC were almost identical and the NIC proved to be homogeneous on immunoelectrophoresis as well as crossed immunoelectrophoresis. But these lectins are turned out as different molecules through the study of carbohydrate specificity. Only NIC lectin was a potent mitogenic toward murine splenic lymphocytes at a concentration ca. 6.4 ㎍/㎖.
콩과 식물에서 분리정제한 렉틴의 생물물리 화학적 연구 ( E - PHA 렉틴 )
전경희,채영흠,서영아,정시련 ( Kyung Hee Jeune - Chung,Young Heum Chae,Young Ah Suh,See Ryun Chung ) 생화학분자생물학회 1983 BMB Reports Vol.16 No.1
Salt fractionated extracts of Phaseolus vulgaris was purified successively through ion exchange chromatography on DEAE Sephadex A-50, hydroxyapatite column and EL-PHA was obtained. EL-PHA was treated with 4M urea just prior to the application into CM-Sephadex C-50 column. This column was eluted with 10 mM (pH 5.7), 20 mM (pH 6.6) and 30mM (pH 8.0) phosphate buffer, each containing 4M urea. In order to identify isolation of E-and L-PHA, erythroagglutination test with human blood A group and lymphoagglutinating test with mouse spleen lymphocytes were measured on each fraction and found three active fractions, L-PHA, having lymphoagglutinating activity only, EI-PHA, having high erythroagglutinating activity only and EII-PHA, having erythroagglutinating activity along with weak lymphoagglutinating activity. In order to characterize biophysicochemical properties of the EI-and EII-PHA, polyacrylamide disc gel electrophoresis, SDS gel electrophoresis, sugar inhibition test, carbohydrate test were performed. In polyacrylamide disc gel electrophoresis, EL-PHA was observed as three bands, EI-and EII-PHA were observed as clear single band with a very faint minor band. Molecular weight of EI-and EII-PHA were estimated at about 130,000 daltons and 125, 000 daltons, respectively by PAGE. The results of SDS-PAGE shown that EI-PHA consists of four homogenous subunits having molecular weight of 34, 000 per unit and EII-PHA consists of two different subunits with 41,000 arid 30,000 daltons. Erythroagglutination by EI-and EII-PHA was inhibited with 0.3% D-mannose and N-acetyl-D-galactosamine, but not with N-galactose, L-fucose, N-acetylneuraminic acid and N-acetyl-D-glucosamine. Sugar components of EI-and EII-PHA were recognized by anthrone test, but no spot was observed in paper chromatography. For immunochemical studies, antisera to EI-PHA were prepared by immunizing rabbit and EI-PHA formed precipitin bands against various antisera in Ouchterlony double immunodiffusion.
장수풍뎅이(Allomyrina dichotoma) 렉틴의 면역기능 증강효과
전경희,정미연,최수정,이종욱,박원학,조세훈,이승호,정시련,Jeune, Kyung-Hee,Jung, Mi-Yeun,Choi, Soo-Jeong,Lee, Jong-Wook,Park, Won-Hark,Cho, Se-Hoon,Lee, Seung-Ho,Chung, See-Ryun 한국생약학회 2001 생약학회지 Vol.32 No.1
A lectin was purified from Allomyrina dichotoma (ADL) by physiological saline extraction, ammonium sulfate fractionation, anion exchange column chromatography on DEAE Sephadex A-50 and gel filtration column chromatography on Sephadex G-200. Several biochemical properties of ADL were characterized as follows: ADL from gel filtration column chromatography showed single band on SDS-PAGE. ADL agglutinated the erythrocytes of rabbit and human A, B, O, AB. Agglutinability was relatively stable at basic pH, and was stable at temperature below $40^{\circ}C$. Agglutinability was not affected by metal ions and EDTA. This lectin was proved to be a glycoprotein which contains 0.47% of sugars. The molecular weight of ADL was estimated to be 97,000 dalton by SDS-PAGE. By amino acid analysis, ADL exhibited high amounts of aspartic acid. The lectin's immunomodulating effect was measured as cytokine production. The productions of 5 cytokines $(IL-1{\alpha},\;IL-2,\;IL-6,\;IFN{\gamma}\;and\;TNF{\alpha})$ from peripheral blood mononuclear cells were measured by ELISA. The lectin induced the highest secretion of IL-2 at 8 hr, $TNF{\alpha}$ at 4 hr, and $IFN{\gamma}$ at 24hr, respectively. These results suggest that ADL can elicit the production of detectable cytokines from PBMC.
사람 말초혈액 단핵세포에서 녹두 렉틴의 사이토카인 생성효과
전경희,안몽기,정수민,최경민,이승호,정시련,Jeune, Kyung-Hee,An, Mong-Gi,Jung, Su-Min,Choi, Kyung-Min,Lee, Seung-Ho,Chung, See-Ryun 한국생약학회 1999 생약학회지 Vol.30 No.4
New lectins have been isolated and purified from mung bean (Phaseolus radiatus) through physiological saline extraction, ammonium sulfate salt fractionation and column chromatographies. Ion exchanger were eluted by linear salt gradient and then further purified through gel filtration. Thus obtained lectin named as MBL. The gene expressions of 5 cytokines (IL-1, IL-2, IL-6, $TNF-{\aphpa}$ and $IFN-{\gamma}$) from human peripheral blood mononuclear cells (PBMC) stimulated with MBL were investigated by using reverse transcription polymerase chain reaction (RT-PCR). PBMC ($1{\times}106$ cells/ml) isolated from healthy volunteers were stimulated with lectins (4 mg/ml) for various time intervals (1 to 96 hrs). After each of the various stimulated times, total RNA was isolated and assessed for different cytokines mRNA by RT-PCR. The mRNA encoding IL-1, IL-2 were detected continuously from 1 to 20 hrs, and IL-6 was detected up to 24 hrs. But the mRNA encoding $IFN-{\gamma}$ and $TNF-{\alpha}$ were detected to 8 hours only and showed short time response compared with other cytokines. The significant expression of all cytokines mRNA were observed at 4 hrs. These results suggested that MBL, as inducer of cytokines could elicit detectable cytokine mRNA from PBMC.
병원성 원생동물의 변이와 약물내성: Leishmania major의 클로로퀸 내성
전경희(Kyung Hee Jeune),정시련(See Ryun Chung),바바라 밀러(Barbara Miller),캐롤 시블리(Carol Sibley) 大韓藥學會 1991 약학회지 Vol.35 No.2
A comparative study was performed on two different strains of Leishmania majorchloroquine sensitive strains (ChlS) and its mutant chloroquine resistant strains (ChlR). ChlR strains were obtained at 5X10-4M chloroquine. Remarkable differences were observed at the initial chloroquine uptake in ChlR and ChlS, ie., the rate of uptake was very reduced in ChlR (Km values were 70nM and 125nM, respectively). Influx and accumulation of chloroquine were also compared between wild type and mutant. An increasing tendency in both influx and accumulation of chloroquine was shown in ChlS, but ChlR demonstrated a rapid release after a little uptake (influx) at the early stage. This result is thought to be basis of their resistance for ChlR strains.
전경희(Kyung Hee Jeune),박채수(Chae Soo Park),박원학(Won Hark Park),최수정(Soo Jeong Choi),소명숙(Myung Suk So),정시련(See Ryun Chung) 대한약학회 1997 약학회지 Vol.41 No.4
A new lectin was partially purified from starfish,Asterina pectinifera by means of physiological saline extraction, salt fractionation, ion exchange chromatography and hydroxyapatite chromatography, and it was named APL. The biochemical properties of the APL were characterized. In addition, its effects on lymphocyte mitogenicity and cancer cell agglutinability were tested. The APL agglutinated nonspecifically human erythrocytes and rabbit blood cells. Agglutinability was decreased to 30% of control activity below pH 5 and above pH 9 and was relatively unstable at increasing temperatures above 60oC. The activity was reduced by addition of two kinds of metal ions, Ba2+, Mn2+ and chelating agent, EDTA. APL was proved to be glycoproteins containing 9% sugars. For carbohydrate specificity, it was found that the activity of APL was inhibited by D(+)-glucosamine, D(+)-galactosamine, stachyose, N-acetyl-galactosamine and methyl-alpha-D-galactopyranoside among 35 sugars tested. In amino acid composition, the contents of acidic amino acids such as aspartic acid and glutamic acid were relatively high. This result suggest that the isoelectric point would be in a lower range. APL was found that it promotes the division of human lymphocytes. APL was proved to be a potent agglutinin for cancer cells such as HeLa, L929 and L1210 cells. Significant changes on the HeLa cell surfaces affected by APL were observed under the electron microscope.
버섯류의 렉틴 성분 개발연구(II) 야생 버섯류의 생리활성 물질, 렉틴 성분 검색
전경희(Kyung Hee Jeune-Chung),김무경(Moo Kyung Kim),정시련(See Ryun Chung) 대한약학회 1987 약학회지 Vol.31 No.4
Twenty species of higher fungi growing in the wild were collected and studied extensively for their lectin activities by using erythrocytes of human, rabbit and mouse blood. In total, 14 species demonstrated hemagglutination with some kinds of erythrocytes. Of twenty species, eight (Boletus edulis, B. splendidus, Clavaria zollingeri, Lactarius subzonarius, L. volemus, Russula cutefracta, Pholiota squarrosa, and P. aspera) were shown lymphoagglutination with murine splenic lymphocytes. Protein contents were estimated from the crude lectin fraction. Above mentioned eight species contained relatively high amounts of proteins than other mushrooms. Since these species had, coincidently, high hemagglutinating activity as well, we could define them as lectin-containing mushrooms. Some species also contained mitogenic lectins toward murine splenic lymphocytes.
별불가사리(Asterina pectinifera) 렉틴의 사이토카인 생성 양상
전경희(Kyung Hee Jeune),최수정(Soo Jeong Choi),정시련(See Ryun Chung) 대한약학회 1999 약학회지 Vol.43 No.4
The purpose of this study is to define whether Asterina pectinifera Lectin (APL) is effective on the cytokine production. Isolated mRNA from hPBMC (human peripheral blood mononuclear cells) stimulated with APL for various reaction times (1 to 96 hours) was detected by RT-PCR. The intensity of band for IL-1 and IFN gamma mRNA was markedly increased at 1 hour, and IL-2 mRNA was strongly expressed at 4 hours. The mRNA band of APL-induced IL-2 and IFN gamma was weaker than that of IL-1, IL-6 and TNF alpha. The mRNA expression of 4 cytokines (IL-1, IL-2, IFN gamma and TNF alpha) was detected up to 48 hours, and that of IL-6 was detected until 72 hours. ELISA was used to look protein secretion of the cytokine gene with IL-1, IL-2 and TNF alpha expressed strongly in RT-PCR. The highest protein secretion was at 4 hours with IL-1, at 8 hours with IL-2 and at 4 hours with TNF alpha. These results suggest that APL can induce the production of some cytokines and the immune response from PBMC was done within the first few hours of stimulation with APL.