• Tuberculosis and Respiratory Diseases
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• v.41 no.3
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• pp.248-261
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• 1994

Background: Lectins are proteins or glycoproteins of non-immune origin that recognize a specific sequence of sugar residues. The availability of a large number of lectins has provided the capacity to identify selectively glycoconjugates possessing distinctive chemical structure in diverse sites of highly specialized biological activity. The purpose of the present study was to investigate the lectin binding patterns of various components in human pulmonary tubercles. Method: Biopsy specimens of tuberculous lung were obtained from male adult patients who underwent a surgical resection for severe pulmonary tuberculosis. The specimens were processed and stained with 13 kinds of biotinylated lectins according to some modification of Hsu and Raine's methods. Results: 1) In the caseous necrotic lesions, BS $I-B_4$ showed negative reaction and BS I were also negative except some irregularly-shaped cells located in the marginal zone. All other lectins, however, showed a positive reaction with various binding patterns. 2) The epithelioid cells were broadly divided into three groups according to the reaction patterns in the cytoplasms and cell membranes. 3) WGA, ECL, PHA-L, PHA-E and LCA showed strong staining in the lymphocytes. 4) SBA showed a different binding patterns between the endothelial layers located in the region beyond the fibrous layers and those located within the fibrous layers. 5) PNA showed a positive reaction in the outer 1/3 to 1/2 of the fibrous layer, but showed no staining in the inner 1/2 to 2/3 of the fibrous layers. Conclusion: The present lectin histochemical study provided a useful information to assess the characterization and distribution of various glycoconjugates in each constituent of human pulmonary tubercles. The results demonstrate structural differences in the glycoconjugate composition of various components of the tubercles and reveal changes in glycosylation in the components during soft tubercle formation. This study provides a new data useful for the studies on the pathogenesis and pathology of human pulmonary tubercles.

• Journal of the korean society of oceanography
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• v.35 no.3
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• pp.153-157
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• 2000

Four different FITC-conjugated lectins were used to visually evaluate lectin binding activity by optical staining quality using confocal laser scanning microscopy (CLSM) of Cochzodinium polykrikoides in nature (wild type) and culture (cultured type). Cells from the field and cultures treated with ConA fluoresced only at the outer cell wall, and the abundance and distribution of the fluorescent signal were similar. Treatment with PWM and HPA did not elicit fluorescence at the cell surface, but the wild type exposed to HPA showed greater binding than did the cultured cells, possibly due to greater concentrations of glucosamine. The wild type cells treated with LBL lectin showed a strong green fluorescence on the cell surface, whereas cultured cells did not. Signal intensity and abundance were greater than for any other lectins tested in this study. These results suggest that wild type and cultured type are significantly different based on surface sugar production. In particular, the wild type cells apear richer in galactosamine-like moieties. Neither glucose nor mannose-like moieties were present in either wild types or cultured cells.

• Proceedings of the KAIS Fall Conference
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• 2007.05a
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• pp.270-272
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• 2007

본 연구는 서산 6쪽 마늘로부터 완전장 유전자 은행의 제작과 이를 통해서 확보된 1,000여개 재조합 클론에 대한 염기서열 결과를 web-based database를 통한 상동성 분석으로 부터 서산 마늘의 발현 유전자에 대한 생물정보학적 분석에 관해 것이며 본 연구로 부터 마늘의 대표적 생리활성 물질인 allicin의 생성에 관여하는 효소인 allinase의 cDNA를 클로닝 및 완전 염기서열을 해석하였으며 allinase 유전자의 genomic structure 에 대한 일부의 결과를 확보하였다. 또한 다양한 생물종에서 연구 되어지고 있는 생리활성 단백질인 lectin 유전자 cDNA를 클로닝하여 완전 염기서멸을 분석하고, 6xHis Tag올 통한 재조합 단백질을 대장균에서 E.coli에서 발현시켰다.

• Proceedings of the PSK Conference
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• 2003.04a
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• pp.217.3-218
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• 2003

A novel lectin has been purified from the fruiting bodies of the mushroom, Fomitella fraxinea, which belongs to bracket fungi by a combination of ion-exchange chromatography on DEAE-cellulose and gel filtration chromatography on Sephacryl S-200 HR. The lectin, designated as FFrL, was a homotetrametric protein with a molecular weight of 50 kDa as demonstrated by SDS-PAGE (sodium dodecyl sulfate-polyacrylamide gel electrophoresis) and MALDI-TOF-MS(matrix assisted UV laser desorption/ionization time-of flight mass spectrometry). (omitted)

• YAKHAK HOEJI
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• v.40 no.4
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• pp.387-393
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• 1996

The erythrocytes agglutination test was applied to the common korean plants for lectin activity screening by using human blood. During the four years, 108 species from 46 families of floras were collected, identified and subjected to the test after being divided into several different parts. Only 13 species demonstrated strong lectin activities. Meanwhile 66 species did not shown any agglutination. All others were observed as having low activity or as having hemolytic constituents.

• Korean Journal of Pharmacognosy
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• v.42 no.1
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• pp.68-75
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• 2011

A new lectin was purified from Bombyx mori (BML) by physiological saline extraction, ammonium sulfate precipitants, anion exchange column chromatography on DEAE Sephadex A-50 and gel filtration column chromatography on Sephadex G-200. BML agglutinated trypsinized and glutaraldehyde-fixed erythrocytes, and was observed the most high activity with rabbit, chicken erythrocytes and rat splenic lymphocytes. Agglutinability was markedly affected at highly acidic pH, but was relatively stable with high temperature. The effect of metal ions was observed and BML was affected by bivalaent cations, especially depending on $Ca^{2+}$, $Fe^{2+}$, $Mn^{2+}$, whereas, inhibited by $Mg^{2+}$. Agglutination was strongly inhibited by heparin and glucuronic acid. BML was proved to be a glycoprotein which contains 17.16% of sugars. By mass spectrometry analysis, we found 2 bands that were considered as lectin subunits.

• YAKHAK HOEJI
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• v.45 no.3
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• pp.302-309
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• 2001

Wheat germ agglutinin (WGA) pectin, which binds to human melanoma cell line, was conjugated with Praecoxin A using 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide as a cross-linking agent. Physical mixture (PM) of WGA and Praecoxin A was also prepared by using a non-specific binding property of Praecoxin A to WGA. The WGA:Praecoxin A ratio in the conjugate and PM was approximately 1:18 and 1:20, respectively. The results of hemagglutination assay and enzyme-linked lectin assay indicated that the conjugate and PM maintained the lectin-like properties of the WGA. The binding ratio of conjugate was about 70% during 4-24 hr, but the most of Praecoxin A was released within 24 hr in the case of PM. These results lead to the conclusion that the conjugate is potentially useful for the formulation of injection that requires targeting for melanoma as well as sustained release at the site.

• Journal of Microbiology and Biotechnology
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• v.11 no.1
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• pp.35-39
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• 2001

A simple method for studying the lectin-like interactions between Helicobacter pylori and cultured human epithelial cell lines was developed using an enzyme-linked, biotin-streptavidin bacterial-adhesion assay. The present study suggests that this method is suitable for evaluating the participation of lectin interactions in the adhesion of H. pylori to cultured HeLa S3 and Kato III cells, both fixed and glycosidase-treated cells, as well as assessing glycoconjugated binding inhibition studies. The time-course and dose-dependent kinetics of the biotin-labeled H. pylori adhesion th the formaldehyde-fixed Hela S3 and Kato III cell lines exhibited saturation. In addition, the binding of the biotin-labeled H. pylori to the formaldehyde-fixed cultured cells was partially blocked by pre-incubation with glycoconjugates and polyclonal antibodies against a heparan sulfate binding protein from H. pylori.

• YAKHAK HOEJI
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• v.31 no.4
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• pp.213-218
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• 1987

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, Lactaritis 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, hiig emagglutinating activity as well, we could define them as lectin-containeing mushrooms. Some species also contained mitogenic lectins toward murine splenic lymphocytes.

• Proceedings of the PSK Conference
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• 2003.10b
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• pp.248.2-248.2
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• 2003

A lectin has been purified from the bark of the legume Maackia fauriei. This lectin, MFA, was found to agglutinate human ABO erythrocytes at a titer of 256. The results from electrophoretic analyses, gel-filtration chromatography, and enzyme linked lectinsorbent assay indicate that MFA is an acidic glycoprotein, and exists as a tetramer of 30 kDa subunits that are linked by noncovalent bonds. The activity of MFA is critically dependent upon CaC1$_2$. MFA demonstrated high homogeneity with the lectins from M. amurensis, which is the only legume source of lectins that bind to sialoglycoconjugate, in its N-terminal amino acid sequence and amino acid composition, (omitted)