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해양 천연물로부터 면역기능 조정제 렉틴 개발: MLA-I, MLA-II, MLA-III의 특성
정시련(See Ryun ChUng),김장환(Jang Hwan Kim),전경희(Kyung Hee Jeune) 대한약학회 1995 약학회지 Vol.39 No.3
Three new lectins, MLA-I, MLA-II and MLA-III, have been isolated and purified from the hemolymph of Meretrix lusoria and reported previously. Biophysicochemical characteristics were investigated with these three MLA lectins. The MLA lectins agglutinated human erythrocytes nonspecifically and proved as D-galactose group carbohydrate specific. Molecular weight of MLA-I, II and III were estimated to be 330, 500 and 31OKD, respectively, by gel filtration on Sepharose CL-6B column. On SDS-polyacrylamide gel electrophoresis, MLA I was dissociated into a single subunit of 42KD, MLA-II was into the twelve subunits of 46, 32, 30, 28, 25, 23, 22, 20, 19, 16, 15, and 14KD, and MLA-III was into the two subunits of 72 and 44KD. The pI of MLA-I, II, III were 4.0, 4.9 and 5.0. Amino acid analysis revealed a high contents of acidic and hydroxy amino acids, and a paucity of sulfur containing amino acids. Proline was not contained in MLA-II.
한국산 식물 자원으로 부터 새로운 렉틴 성분의 분리 정제 ( 1 ) 콩과 식물의 렉틴
정시련,전경희 ( See Ryun Chung,Kyung Hee Jeune Chung ) 생화학분자생물학회 1981 BMB Reports Vol.14 No.3
In order to find new lectins from Korean natural products, 55 kinds of plants belonging to 31 families were screened by using several different type of blood cells. Phaseolus vulgaris C(W, K. B.) and Cercis chinenesis of Leguminosae contained strong hemagglutinating proteins. The crude lectins from W. K. B. were purified by DAEA Sephadex A-50 column chromatography. The 0.1 M peak from this procedure demonstrated acceptable criteria, e. g. yield, optical density and hemagglutinating activity and three bands were observed in polyacrylamide disc gel electrophoresis. A further purification was achieved by hydroxyapatite column chromatography and strong hemagglutinating activity was recovered in 0. 1 M peak. It was elecrophoresed and found to migrate as a single bans. The condition of purification for W. K. B. lectin was encourageabie but did not brought agreeable satisfaction to the Cercis chinensis lectin.
정시련,베르나 듀랑 ( See Ryun Chung,Bernard Durand ) 생화학분자생물학회 1977 BMB Reports Vol.10 No.3
The binding interactions between cytokinin analogs and ribosomes of a dioecious plant are studied. Molecular interactions between cytokinins and ribosomes have been investigated and compared to male and female by using radioactively labeled 6-benzylamino [8-^(14)C] purine as a probe. Further results on the binding of benzylaminopurine to male ribosomes in connection with kinetin, 6-furfurylaminopurine, and their respective ribosides are reported presently.
Cytokinins Binding to Dioecious Plant Ribosomes
정시련,베르나듀랑,Chung, See-Ryun,Durand, Bernard 생화학분자생물학회 1977 한국생화학회지 Vol.10 No.3
사이토 카이닌 유도체와 자웅이주 식물의 라이보좀과의 결합에 관한 연구로서 방사성화합물 6-benzylamino[8-$^{14}C$]purine을 조사수단으로 이용하여 이것과 남성 및 여성 라이보좀과의 분 결합에 관한 결과를 보고한 바 있다. 이 연구는 한걸음 더 나아가 benzylaminopurine과 furfurylaminopurine (kinetin) 및 이들 각각의 riboside가 남성 라이보좀과 결합하는 상호 관계를 밝혀보고저 하는 것이다. The binding interactions between cytokinin analogs and ribosomes of a dioecious plant are studied. Molecular interactions between cytokinins and ribosomes have been investigated and compared to male and female by using radioactively labeled 6-benzylamino [8-$^{14}C$] purine as a probe. Further results on the binding of benzylaminopurine to male ribosomes in connection with kinetin, 6-furfurylaminopurine, and their respective ribosides are reported presently.
정시련,손경숙,소명숙,전경희,Chung, See-Ryun,Son, Kyeun-Suk,So, Myung-Suk,Jeune, Kyung-Hee 생화학분자생물학회 1987 한국생화학회지 Vol.20 No.3
밤고둥의 생리식염수용액 추출물은 사랑 및 각종 동물 적혈구를 비특이적으로 응집시켰으며 림프구도 응집시켰다. 밤고둥의 새로운 렉틴 성분을 생리식염수용액추출, 황화암모늄 침전, 이온교환 크로마토그래피 등의 방법으로 분리 정제하였다. 이는 전기영동상에서 하나의 주된 띠와 다른 몇개의 띠를 나타내었으며 주된 띠에서만 렉틴활성을 나타냈다. 부분 정제된 밤고둥 렉틴은 pH변화에는 비교적 안정하였으나 열에는 불안정하였다. 적혈구 응집은 lactose와 D-galactose의 각각 10mM과 100mM농도에서 저해되었다. 또한 밤고둥 렉틴은 마우스의 림프구에 대한 분열자극효과를 나타냈다. The whole body extracts of a top shell, Chlorostoma argyrostoma lischkei, agglutinated nonspecifically human and other animal erythrocytes and also agglutinated rat and murine splenic lymphocytes. New lectin was purified by the following procedures: 0.15M NaCl extraction, salt fractionation and ion exchange column chromatographies. The purified lectin showed one major and a few minor bands in polyacrylamide gel electrophoresis, but in only one major band had lectin activity. The partially purified lectin was relatively stable at various pH, but heat labile. Among the tested sugars, only lactose and D-galactose inhibited lectin activity at a concentration of 10mM and 100mM, respectively. The lectin was a mitogenic toward murine splenic lymphocytes
The Influence of Mineral Nutrients on Growth and Alkaloid Levels in Lycopersicum esculentum
정시련(See-Ryun CHUNG) 한국식품영양과학회 1972 한국식품영양과학회지 Vol.1 No.1
Twenty kinds of minerel nutrient solution were prepared and supplied to the tomatoes planted in Norwegian quartz pots.<br/> These plants were cultured for nine weeks and several physiogical phenomena were observed duirng the growing period, and after harvest, the alkaloid contents were determined.<br/> The highest growth potential was in NS 3 group while the highest alkaloid content wasein KMg 18 group.
해양패류로부터 렉틴성분 개발연구 조각매물고둥 렉틴의 분리 , 정제 및 특성
정시련,김장환,전경희 ( See Ryun Chung,Jang Hwan Kim,Kyung Hee Jeune - Chung ) 생화학분자생물학회 1985 BMB Reports Vol.18 No.4
A New lectin from shellfish, Neptunea intersculpta, was purified by the following steps; 0.15 M NaCl extraction, (NH₄)₂SO₄ precipitation, DEAE-cellulose, hydroxyapatite and gel filteration on Sephadex G-100 column chromatography. The NIA (Neptunea intersculpta)lectin was shown one major band and two faint minor bands on polyacrylamide gel electrophoresis. Agglutinating activity was specifically inhibited by lectose and no carbohydrate was found by anthrone test and thin layer chromatography. Immunochemical techniques were employed to examine structural similarities between NIA lectin and other crude lectin. The result of immunodiffusion showed that NIA lectin was partialy identified with white kidney bean crude lectin, but was not identified with Agaricus bisporus crude lectin. Further characterization of the biological and chemical properities of this lectin are still in progress.
정시련(See Ryun Chung),김장환(Jang Hwan Kim),소명숙(Myung Suk So),김무경(Moo Kyung Kim),현태금(Tae Geum Hyun),전경희(Kyung Hee Jeune) 大韓藥學會 1991 약학회지 Vol.35 No.5
Two kinds of new lectin fractions (LOA-I, LOA-II) were obtained from loach (Misgurnus spp.) meat by 0.15 M NaCl extraction, salt fractionation, ion exchange and hydroxyapatite column chromatographies. On polyacrylamide gel electrophoresis, LOA-I exhibited one major and a few minor bands, but LOA-II exhibited three minor bands. The partially purified loach lectins agglutinated not only erythrocytes of human B and AB type, rabbit, dog, but also murine splenic lymphocytes. Agglutinability was relatively labile at various pH and stable at increasing temperature, but was not affected by tested several metal ions. By the sugar specificity test, D-glucosamine and methyl-beta-galactopyranose inhibited agglutinating activity at a final concentration of 3 mM. The lectins contained relatively high amounts of aspartic acid, valine and leucine, but sulfur containing amino acids, cystein, methionine and isoleucine were not determined. LOA-I, LOA-II lectins were nonmitogenic toward murine lymphocytes.