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해양 천연물에서 분리한 면역기능 조정제 렉틴 MLA의 림프구 자극분열효과 및 면역화학적 특성
전경희(Kyung Hee Jeune),김장환(Jang Hwan Kim),정시련(See Ryun Chung) 대한약학회 1995 약학회지 Vol.39 No.3
Isolation, purification and characterization of biophysicochemical properties of the three new lectins. MLA-I, MLA-II, MLA-III from the hemolymph of Meretrix lusoria have been reported previously. A series of immunochemical studies were investigated in this work. The three lectins were revealed as having partial identity each other by immunodiffusion and immunoelectrophoresis. These results suggest that MLA lectins are isolectins having similar biophysicochemical properties. Particularly, MLA-I proved to be a potent mitogen for murine splenic as well as human peripheral lymphocytes, and the optimum mitogenic dose were 62.5 and 1.95mcg/ml, respectively.
해양패류 렉틴 ( Ⅸ ) 백합조개 체액 렉틴 , MLA - 1의 분리정제 및 당 특이성
김장환,정시련,전경희 ( Jang Hwan Kim,See Ryun Chung,Kyung Hee Jeune ) 생화학분자생물학회 1990 BMB Reports Vol.23 No.3
D-fucose, L-arabinose, D-galacturonic acid and D-glucuronic acid specific lectin (MLA-1) has been purified from the hemolymph of a shellfish Meretrix lusoria (Veneridae) using ion exchange chromatography on DE 52, hydroxyapatite and gel filtration. The MLA-1 lectin agglutinatinted nonspecifically erythrocytes of human ABO blood type and of several animals. In carbohydrate inhibition assay, MLA-1 lectin activity was most strongly inhibited by three carbohydrates, D-fucose, L-arabinose and D-galacturonic acid, whose pyranose rings share the same configuration as the C2, C3 and C4. A molecular weight of MLA-1 was calculated as 330 Kd by gel filtration on Sepharose CL-6B column and the subunit was determined as 42 Kd by SDS-PAGE.
백합조개 체액으로부터 새로운 렉틴 MLA-II 및 MLA-III의 정제
김장환,정시련,전경희,Kim, Jang-Hwan,Chung, See-Ryun,Jeune, Kyung-Hee 대한약학회 1994 약학회지 Vol.38 No.4
As a previous step for the development of immunostimulating substance from marine natural products the two new lectins, MLA-II and MLA-III, have been isolated and purified from the hemolymph of Meretrix lusoria in addition to the previously reported MLA-I. The new lectins molecules were characterized as pure by electrophoretic studies.
김장환,정시련,전경희,Kim, Jang-Hwan,Chung, See-Ryun,Jeune, Kyung-Hee Korean Society for Biochemistry and Molecular Biol 1990 한국생화학회지 Vol.23 No.3
D-fucose, L-arabinose, D-galacturonic acid, D-glucuronic acid에 특이성인 렉틴(MLA-1)을 이온 교환, Hydroxyapatite 크로마토그래피 및 겔 여과법을 이용하여 백합조개, Meretrix lusoria(Veneridae), 체액으로부터 분리 정제하였다. MLA-1 렉틴은 사람 혈액 ABO type과 몇 종의 동물 혈액에 비특이적인 것으로 밝혀졌다. 당 저해시험에서, MLA-1 렉틴 응집은 pyranose ring이 2,3,4번 탄소에 대해 같은 구조인, D-fucose, L-arabinose, D-galacturonic acid, 세 가지 당에 의해 가장 강하게 저해되었다. MLA-1 렉틴의 분자량은 Sepharose CL-6B 겔여과 결과 330 Kd, SDS-PAGE에 의한 subunit의 수와 크기는 단일의 형태이었으며 그 분자량은 42 Kd로 밝혀졌다. D-fucose, L-arabinose, D-galacturonic acid and D-glucuronic acid specific lectin (MLA-1) has been purified from the hemolymph of a shellfish Meretrix lusoria (Veneridae) using ion exchange chromatography on DE 52, hydroxyapatite and gel filtration. The MLA-1 lectin agglutinatinted nonspecifically erythrocytes of human ABO blood type and of several animals. In carbohydrate inhibition assay, MLA-1 lectin activity was most strongly inhibited by three carbohydrates, D-fucose, L-arabinose and D-galacturonic acid, whose pyranose rings share the same configuration as the C2, C3 and C4. A molecular weight of MLA-1 was calculated as 330 Kd by gel filtration on Sepharose CL6B column and the subunit was determined as 42 Kd by SDS-PAGE.
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.
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.
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.
해양 패류 렉틴성분 연구(V) 반지락조개의 렉틴성분 분리정제에 관한 연구
정시련(See Ryun Chung),김장환(Jang Hwan Kim),전경희(Kyung Hee Jeune-Chung) 대한약학회 1987 약학회지 Vol.31 No.2
The result of the screening of lectins on 28 species of marine shell fishes (mollusks) showed that 10 species (Tapes philippinarum, Cyclosunetta menstrualis, Neptunea arthritica cumingii, Omphalius pfeifferi carpenteri, Chlorostoma argyrostoma turbinatum, Chiorostoma argyrostoma lischkei, Semisulcosira corea, Neptunea polycosta, Babylonica japonica, Noverita didyma) were present hemagglutinating properties to human A, B, and 0 group, and animal blood erythrocytes. A new lectin from Tapes philippinarum was isolated and partially characterized. The lectin was purified by (NH4)2SO4 precipitation and ion exchange chromatography on DE 53 column. Six fractions were obtained from DE 53 column by salt gradient elution but only 0.3M, and 0.4M NaCl fraction had strong lectin activity. On its 0.3M NaCl fraction, purity was identified by polyacrylamide gel electrophoresis. This lectin was inhibited by N-acetyl-D-galactosamine. It seems that two kinds of lectin react as antigen by immunochemical studies.
해양 천연물에서 분리한 면역기능 조정제 렉틴 MLA의 림프구 자극분열효과 및 면역화학적 특성
전경희,김장환,정시련 영남대학교 약품개발연구소 1995 영남대학교 약품개발연구소 연구업적집 Vol.5 No.-
Isolation. purification and characterization of biophysicochemical properties of the three new lectins. MLA-Ⅰ, MLA-Ⅱ, MLA-Ⅲ from the hemolymph of Meretrix lusoria have been reported previously. A series of immunochemical studies were investigated in this work. The three lecins were revealed as having partial identity each other by immunodiffusion and immunoelectrophoresis. These results suggest that MLA lectins are isolectins having similar biophysicochemical properties. Particularky. MLA-Ⅰ proved to be a potent mitogen for murine splenic as well as human peripheral lymphocytes, and the optimum mitogenic dose were 62.5 and 1.95 ㎎/ml, respectively.