• Proceedings of the Korean Society of Fisheries Technology Conference
• /
• 2001.05a
• /
• pp.146-147
• /
• 2001

Lectins or carbohydrate-binding proteins are proteins of non-immune origin, which is able to agglutinate cells, and precipitate polysaccharides and glycoconjugates (Goldstein et al., 1980). Lectins with diverse physiological roles are widely distributed to the various plant, microorganisms, invertebrates and vertebrates. The ubiquitous occurrence of lectins in nature and their ability to recognize complementary sugars provided a stimulus for the continuous research for their biochemical properties and physiological functions (Raz and Lotan, 1987). (omitted)

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

• YAKHAK HOEJI
• /
• v.27 no.3
• /
• pp.221-227
• /
• 1983

New lectins, lymphoagglutinating lectins from mung beans (MBLA) have been isolated and purified. Mung beans crude extracts were made with 0.15M NaCl and these were purified through anionic exchange chromatography. Four fractions were obtained from DEAE Sephadex A-50 by salt gradients elution. Lectin activity, enzyme activity, protein assay, identification of purity by polyacrylamide gel electrphoresis and immunochemical studies were carried out with these four fractions. Through these results, it can be suggested that 0.2M fraction is newly found potent MBLA. There were some relationships with MBLA and L-PHA but no similarities were observed between MBLA and E-PHA.

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

• IMMUNE NETWORK
• /
• v.7 no.4
• /
• pp.197-202
• /
• 2007

Background: Immunomodulators enhancing MHC-restricted antigen presentation would affect many cellular immune reactions mediated by T cells or T cell products. However, modulation of MHC-restricted antigen presentation has received little attention as a target for therapeutic immunoregulation. Here, we report that lectins isolated from mushroom Fomitella fraxinea enhance MHC-restricted exogenous antigen presentation in professional antigen presenting cells (APCs). Methods: Lectins, termed FFrL, were isolated from the carpophores of Fomitella fraxinea, and its effects on the class I and class II MHC-restricted presentation of exogenous ovalbumin (OVA) were examined in mouse dendritic cells (DCs) and mouse peritoneal macrophages. The effects of FFrL on the expression of total MHC molecules and the phagocytic activity were also examined in mouse DCs. Results: DCs cultured in the presence of FFrL overnight exhibited enhanced capacity in presenting exogenous OVA in association with class I and class II MHC molecules. FFrL increased slightly the total expression levels of both class I (H-$2K^b$) and class II (I-$A^b$) MHC molecules and the phagocytic activity of DCs. Antigen presentation-enhancing activity of FFrL was also observed in macrophages isolated from mouse peritoneum. Conclusion: Lectins isolated from the carpophores of Fomitella fraxinea increase MHC-restricted exogenous antigen presentation by enhancing intracellular processing events of phagocytosed antigens.

• Asian Pacific Journal of Cancer Prevention
• /
• v.17 no.9
• /
• pp.4185-4197
• /
• 2016

Chronic arsenicosis is a major environmental health hazard throughout the world, including India. Animals and human beings are affected due to drinking of arsenic contaminated ground water, due to natural mineral deposits, arsenical pesticides or improperly disposed arsenical chemicals. Arsenic causes cancer with production of free radicals and reactive oxygen species (ROS) that are neutralized by an elaborate antioxidant defense system consisting of enzymes and numerous non-enzymatic antioxidants. Dietary antioxidant supplements are useful to counteract the carcinogenesis effects of arsenic. Oyster mushroom lectins can be regarded as ingredients of popular foods with biopharmaceutical properties. A variety of compounds have been isolated from mushrooms, which include polysaccharides and polysaccharopeptides with immune-enhancing effects. Lectins are beneficial in reducing arsenic toxicity due to anticarcinogenetic roles and may have therapeutic application in people suffering from chronic exposure to arsenic from natural sources, a global problem that is especially relevant to millions of people on the Indian subcontinent.

• ALGAE
• /
• v.24 no.1
• /
• pp.39-45
• /
• 2009

The conjugation processes of a filamentous freshwater green alga Spirogyra varians were examined using FITC-lectins. Conjugation comprised five steps: 1) aligning with adjacent filaments, 2) formation of conjugation protru-sion (papilla), 3) fusion of the protrusions, 4) formation of conjugation tube,and 5) formation of zygotes. Three lectins, ConA, RCA and UEA, showed considerable labeling during the progression of conjuation. FITC-ConA labeled the surfaces of filaments throughout the whole conjugation processes. FITC-RCA labeling was observed at the conjugation protrusions only after the papilla formation. Strong labeling continued until formationg of zygotes at the contacting area where the conjugation tube developed, but no labeling was detected on the surface of vegetative filaments. The labeling decreased gradually over time and disappeared when zygotes were formed. FITC-UEA showed similar labeling pattern with FITC-RCA except that weak labeling remained after zygote formation. Inhibition experiments using RCA, UEA which are complementary to sugars L-fucose and D-galactose, showed considerable decrease of conjugation (<32% vs. 70% in control). These results suggested that the lectin-carbohydrate recognition system might be involved in the conjugation of spirogyra varians.

• Journal of the korean society of oceanography
• /
• v.34 no.3
• /
• pp.167-171
• /
• 1999

Since toxic Alexandrium catenella and non-toxic A. fraterculus are morphologically similar, they are difficult to discriminate under the light microscope. However, a novel technology, such as fluorescein isothiocyanate (FITC)-conjugated lectin probes enables easy and rapid differentiation. Toxic A. catenella bound seven different lectins, whereas the non-toxic A. fratercuzus did not bind Arachis hypogaea (PNA) lectin. In addition, Pseudo-nitrschia species in this study were also difficult to identify to species level with light microscope techniques, but it was possible to classify them using fluorescent lectins. Pseudo-nitzschia multistriata, P. subfraudulenta and P. pungens bound Canavalia ensiformis (ConA), whereas P. subpaclfica did not, and P. pungens also bound Ricinus communis (RCA). These results imply that lectin could be used as a critical tool in the differentiation of P. multistriata, P. subfraudulenta and P. pungens. However, P. subpacifica was not differentiated by the lectins tested. Therefore, it isconcluded that lectin probes are useful for discriminating toxic A. catenella from non-toxic A. fraterculus, and for the identification of some Pseudo-nitzschia species. In addition, this method has a great potential to speed and detection between non-toxic and toxic harmful algal blooms (HABs) in Korean biotoxin monitoring systems.

• Proceedings of the PSK Conference
• /
• 2002.04a
• /
• pp.79-80
• /
• 2002

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.23 no.3
• /
• pp.515-519
• /
• 1994

The ComparativThe comperisons of Kintoki bean lectin (KBL) and Taro tuber lectin (TTL) which have been studied in our laboratory are summerized. The recoveries of pure lectins are 0.12% and 0.014%, respectively. They seems to have slight differences in isoelectric points(pH) ; 5.19~5.67 for KBL and 6.41~7.42 for TTL. The minimum concentrations of HA are $2.8\mu\textrm{g}/ml\;and\;21.6\mu\textrm{g}/ml$. The enzymatic modification on HA, growth inhibition, inhibition of nutritional absorption and binding capacities (FITC, $^3H$) of KBL are demonstrated to be much greater than those of TTL.