• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.4
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• pp.494-499
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• 1993

The morphological and histochemical observation of the lectin binding to intestine in vivo or in vitro was investigated. Our finding demonstrates the validity of semi-quantitative estimates of lectin binding to mouse intestine. The fluorescence patterns obtained after treatment of intestine sections with FITC-conjugated lectin revealed that Kintoki bean lectin (KBL) and Taro tuber lectin (TTL) were localized on the cell membrane, especially the top and upper sites of the villi and showed that KBL was more strongly located than TTL under various conditions. In the reverted intestine of mice fed lectin, the villi were considerably disordered and conspicuously disrupted.

• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.4
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• pp.489-493
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• 1993

The major objective of this study carried out was to compare the binding of Kintoki bean lectin (KBL) and Taro tuber lectin (TTL) to the mouse intestinal segments using $^3$H-labeled lectins and to assess the effect of such binding on the ability of the small intestine. Binding of $^3$H-KBL or $^3$H-TTL was studied under various conditions of time course, temperature, concentration, pH and additives of sugars, EDTA or unlabeled native lectin. The interaction of the lectins to intestinal tissue was stronger in KBL than in TTL, which was supposed to be the major reason for the stronger antinuritional enen of KBL. The optimal binding conditions were at 37$^{\circ}C$ for 60mins and at pH 7. The binding of both lectins were inhibited by fetuin and EDTA.

• Proceedings of the Korean Society of Fisheries Technology Conference
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• 2000.05a
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• pp.530-530
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• 2000

The host defense system or immune system of all modern animals has their roots in very ancient organisms. After analyzing literature data concerning properties of invertebrates and vertebrates lectins we suggest that mechanism of mannans recognition may exist in marine invertebrates, as a universal mechanism for homeostasis maintenance and host defense, and mannan-binding lectins family of vertebrates has ancient precursor, as was shown for another S-type lectins family. We carried out the screening of mannan-binding type lectin among different species of echinoderms inhabiting in Piter the Grate Bay, the sea of Japan. As a result, the C-type lectins (SJL-32) specific for high mannose glycans was isolated from the coelomic plasma of the sea cucumbers Stichopus japonicus by ion-exchange chromatography on a DEAE-Toyopearl 650M, affinity chromatography on a mannan-Sepharose 6B and gel filtration on a Sephacryl S-200. SJL-32 is homodimer with molecular mass about 32 kDa on SDS-PAGE under non-reducing conditions. Protein part of the lectin has high conteins Asn, Glu, Ser. Hemagglutination of trypsin-treated O blood group human erythrocytes by SJL-32 was competitively inhibited by high-branched -D-mannan composed of -1,2 and -1,6 linked D-mannopyranose residues. In contrast, a variety of mono-, oligo-, and polysaccharides composed of residues of galactose and fucose showed absence or little inhibitory activities. The lectin activity strong depends on Ca2+ concentration, temperature and pH. Monospecific polyclonal antibodies were obtained to the lectin. As was shown by ELISA assay, antibodies to SJL-32 cross-reacted with human serum mannan-binding lectin. This data allows making conclusion about common antigenic determinants and structural homology of both lectins. In our opinion, SJL-32 belongs to evolutionary high conservative mannan-binding lectins (MBLs) family and takes part in the host defense against pathogenic microorganisms.

• Journal of Pharmaceutical Investigation
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• v.22 no.2
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• pp.155-161
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• 1992

Although glycosylated liposomes have attracted much attention as targeting delivery systems (DDS) of drugs to specific organs which have glycoside receptors, physical instability of liposomes greatly limits their practical application. In this case, proliposomes might be a potential answer to solve this problem. Utilizing the proliposomes as tageting DDS has been a goal of our series of works; we have tried to develop DDS which form liposomes uppon adding water and can deliver drugs to specific target organs/cells such as hepatocytes. In this paper, preparation of glycosylated liposomes and binding of the liposomes with lectin (agglutinin RCA 120) was studied. Asialoletuin (AF) was selected as a model compound which has galactose terminal and is favorable for binding with galactose receptor on the surface of hepatocytes. AF was obtained by splitting the terminal N-acetylneuraminic acid (NANA) of fetuin. Small unilamellar AF-liposomes were prepared by mixing aqueous solution of AF-palmitate with thin film of phosphatidyl choline and cholesterol (30:10 w/w) formed on the innersurface of the round bottomed flask. They were successively extruded through polycarbonate membranes (0.45 mm). Palmitoyl-AF not incorporated into the liposomal bilayer was separated from liposomes by a Sepharose 4B column equilibrated with 10 mM Tris-HCI buffered saline. Lectin (agglutinin RCA 120) was added to the suspension of AF-liposomes and incubated at $37^{\circ}C$ for 2 hr. After centrifugation, the unbound lectin in the supernatant was assayed for protein. The binding of the lectin to AF-liposomes (AF content 2.8 nmole) at $37^{\circ}C$ was linear at least upto 35 mg of lectin indicating high affinity association of the lectin to AF molecules of the liposomes.

• Fisheries and Aquatic Sciences
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• v.3 no.2
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• pp.83-87
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• 2000

We have investigated lectin binding patterns in order to apply binding records of previous laboratory experiments to field settings before the first ourbreaks of harmful algal bloom (HAB). Although cells were grown under different conditions, the binding patterns were the same as in the control. In addition, culture days was not associated with the binding patterns, when compared with the control. In nature, this results suggest that ECA, HPA and WGA lectin are able to discriminate between C. polykrikoides and G. impudicum, as well as ECA and SBA have a capability as a tool for differentiating between C. polyrikoides and G. catenatum, although these species are closely similar under the light microscope fiexed with Lugol solution.

• Journal of Life Science
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• v.19 no.2
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• pp.284-288
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• 2009

The innate immune system is important for the first line of host defence against infectious agents, which have penetrated the mechanical barriers. Mannose-binding lectin (MBL or mannan-binding protein, MBP) is a serum protein that is synthesized in the liver as a part of the acute phase response. MBL binds to carbohydrate structures presented by a wide range of pathogenic bacteria, viruses, fungi, and parasites. MBL is synthesized as a monomer that has a carboxy-terminal carbohydrate recognition domain, a neck region and a collagen region. Low MBL level was reported to be the most frequent immuno-deficiency syndrome. Although extensive studies have yielded detailed information on the structure of MBL, functions of the MBL complex are not fully understood yet. We, here, present cloning process of MBL cDNA from the rat liver and production of truncated recombinant MBL protein using a bacterial expression system in order to produce anti-MBL polyclonal antibody. Anti-MBL polyclonal antibody was raised in a New Zealand rabbit and its affinity was tested against recombinant protein using western blot technique. MBL cDNA, recombinant protein and anti-MBL antibody could be used as great arsenals to dissect cellular biochemistry of MBL.

• Journal of Life Science
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• v.20 no.9
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• pp.1420-1425
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• 2010

Innate immunity is the first line of host defense consisting of various molecules against infectious challenges. Mannose-binding lectin (MBL) belongs to the collectin protein family which takes part of innate immunity and is able to recognize specific carbohydrates on the surface of a variety of infectious agents acting as a pattern recognition molecule. In this way, MBL differentiates self from non-self and interacts with other molecules of the immune system. MBL genotype shows various MBL2 polymorphisms which are responsible for MBL deficiency in a substantial portion of the entire human population and for susceptibility to infectious disease. Therefore, it has been highlighted in the relationship between genetic variants and clinical significance. Here we focus on presenting anoverview of our understanding of MBL structure and functions.

• Journal of Life Science
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• v.14 no.3
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• pp.417-424
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• 2004

This study attempts to investigate lectin binding patterns of the glycoconjugates of the esophageal mucous cells in four teleostean speceis, i. e., Sebastes schlegeli, Halichoeres poecilopterus, Bryzoichthys lysimus and Takifugu pardalis. To investigate glycoconjugates of esophageal mucous cells, nine biotinylated lectins (DBA, SBA, PNA, BSL-l, RCA-l, sWGA, UEA-l, LCA and ConA) were applied with ABC method. Esophageal mucous cells of Sebastes schlegeli and Halichoeres poecilopterus were mixed with large, medium sized and small mucous cells. But these cells of the other species only were mixed with medium sized and small mucous cells. The lectin binding pattern of esophageal mucous cells depends on the species; Sebastes schlegeli was stained with DBA, SBA, BSL-l, RCA-l and sWGA, Halichoeres poecilopterus with DBA, SBA, PNA and sWGA, Bryzoichthys lysimus with SBA and sWGA, Takifugu pardalis with all lectins except DBA, LCA and Con A, respectively. All the mucous cells of Sebastes schlegeli were stained with DBA, SBA and sWGA, while small mucous cells with BSL-l besides these lectins. In Halichoeres poecilopterus,l the large mucous cells reacted with PNA, medium sized mucous cells with DBA, SBA and sWGA, and small mucous cells with DBA and SBA, respectively. Medium sized mucous cells of Bryzoichthys lysimus were stained with sWGA, and small mucous cells with SBA and sWGA. In Takifugu pardalis, all mucous cells reacted with SBA, PNA and RCA-l, but medium sized mucous cells with sWGA and UEA-l besides these lectins. Especially DBA and SBA lectins showed a strong binding to all mucous cells of Sebastes schlegeli. In Halichoeres poecilopterus, PNA binding were notable in large mucous cells, and SBA binding in medium sized and small cells, respectively. However, SBA, PNA, sWGA and UEA-l lectins of Takifugu pardalis showed a strong binding to medium sized mucous cells, but RCA-l binding which small mucous cells were notable.

• Current Research on Agriculture and Life Sciences
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• v.15
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• pp.25-32
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• 1997

This study was carried out to research the biological characteristics among rhizobia and soybean seed and root lectins, and to obtain a basic imformation of host specificity in biological nitrogen symbiosis system. The results obtained were as follows: Purified seed lectin from soybean varieties of paldal, backwoon and hwangkeum formed immunoprecipitin lines with standard soybean seed lectin and the root lectins from soybean seedlings immunoelectrophoretically. Soybean seed and root lectins interacted with Rhizobium japonicum and Bradyrhizobium japonicum, but didn't interacted with Rhizobium. viceae, whereas pea lectin conjugated with R. viceae, but didn't bind with R. japonicum and B. japonicum. Lipopolysaccharides of B. japonicum and R. viceae were fractionated into LPS I and LPS II on the sephadox G-50. Lipopolysaccharides from B. japonicum showed rhe binding acitivity both with soybean seed lectin and root lectin, but those from R. viceae didn't show it with soybean seed and root lectins.

• Korean Journal of Veterinary Research
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• v.36 no.3
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• pp.531-539
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• 1996

The lectin-binding patterns in the testis of the sexually matured Jindo dog were investigated to study the distribution of glycoconjugates in the seminiferous tubule under light and transmission electron microscopy. Positive reactions to Wheat germ agglutinin(WGA) and Dolichos biflorus agglutinin (DBA) were observed in the Sertoli cell and in the residual body of spermatid with a stronger reaction in the Sertoli cell to the lectins than in the residual body. Strong reactions to Soybean agglutinin(SBA) and Peanut agglutinin(PNA) were observed in the acrosome vesicles of the Golgi- and cap-phase spermatid, while a moderate reaction was observed in the acrosome-phase, maturation-phase spermatid and the residual body. The acrosome area of the spermatid reacted intensively to Griffonia simplicifolia agglutinin( GS-I) when the cell was in the acrosome-phase and maturation-phase, and the same reaction to the GS-I was observed in the residual body. However, the seminiferous tubule did not react to Ulex europeus agglutinin I(UEA-I). The gold-labelling of the Sertoli cells with DBA resulted in positive reactions of the Sertoli cell column and processes when observed under the electron microscopy, while the Golgi-, cap- and acrosome-phase spermatids reacted positively to SBA in the peripheral low-dense area of the acrosome vesicle of spermatid. Based on these results, we concluded that differences in the lectin-binding pattern of the seminiferous tubules were recognized in the Jindo dog compared to other animals.