• YAKHAK HOEJI
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• v.35 no.5
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• pp.444-455
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• 1991

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 metyl-$\beta$-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.

• YAKHAK HOEJI
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• v.39 no.1
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• pp.24-30
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• 1995

Lectin from mistletoe(Viscum coloratum) fermented by Lactobacillus plantarum was compared with the lectin from unfermented mistletoe. Agglunating activity of fermented mistletoe was stable at pH 3.77~8.71, at temperature range of $0~40^{\circ}C$ and in the presence of 9 mental ions, which results are similar to unfermented one, but less stable at pH 2.03~3.00 and more stable at temperature $60~80^{\circ}C$ than lectin from unfermented one. Agglunating activity of lectin from mistletoe fermented for 1 or 2 days and from fraction number 42~54 was not inhibited by all sugars used except for lectin from fraction number 21~34. Mitogenic activity to murine lymphpocytes of lectin from mistletoe was decreased by fermentation process.

• Applied Microscopy
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• v.23 no.2
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• pp.84-96
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• 1993

This study was to investigate the effects of maternal diabetes on the lung tissue of the fetal rat using lectin histochemistry and electron microscope technique. Maternal diabetes was induced by intraperitoneal injection of streptozotocin (75 mg/kg the body weight) into pregnant Sprague-Dawley rats on the 7th day of gestation. Fetuses of streptozotocin induced diabetic rats exhibited delayed lung maturation and reduced air space. In lectin histochemistry, the binding of Maclura pomifera (MPA) to fetal lungs from diabetic mothers was reduced, but no significant changes in the bindings of Concanavalin A (Con A), Wheat germ agglutinin (WGA), Ricinus communis I (RCA I) and Griffonia simplicifolia (GSI-$B_4$) were noted. Because the MPA has affinity to terminal N-acetyl-D-galactosamine residues constantly linked O-glycosidically to serine or threonine, the present findings may indicates that maternal diabetes interfere with the processes of O-linked glycosylation in fetal rat lung.

• Korean Journal of Food Science and Technology
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• v.41 no.5
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• pp.560-565
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• 2009

In this study, Korean mistletoe extract (KM-110) was fermented with two strains of Lactobacillus (FKM-110) and then toxicity, lectin content, and immune activities were investigated. The lectin content of FKM-110 was about 53-71% lower than that of KM-110. When mice were subcutaneously administered with KM-110 and FKM-110, the $LD_{50}$ obtained for KM-110 treatment was 50-100 mg/kg as compared to 150-200 mg/mL for FKM-110. Each preparation stimulated macrophages directly and enhanced productivity of inflammatory cytokines such as TNF-${\alpha}$ and IL-$1{\beta}$. FKM-110 treatment resulted in lower cytokine production compared to KM-110. When mice were immunized with Keyhol limpet hemocyanin (KLH) antigen along with KM-110 or FKM-110 administration, higher antibody titers to KLH were observed in the KM-110 or FKM-110 groups compared to mice immunized with KLH alone, thereby showing no difference between KM-110 and FKM-110. Therefore, fermentation of Korean mistletoe extract with these Lactobacillus strains decreased toxicity in vivo while the enhancement of immune activity by KM-110 and FKM-110 was similar. These data suggest that KM-110 fermentation tended to decrease lectin content and in vivo toxicity. In addition, other components in the fermented mistletoe extract appear to stimulate immuno-adjuvant activity instead of lectin.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.68 no.3
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• pp.114-120
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• 2023

Soybean is the one of the most important crops for providing quality vegetable protein to umans and livestock. Soybean cultivars with a brown seed coat have a wide range of antioxidant benefits because of the flavonoid components. However, they also contain lectin, 7S α′ subunit, lipoxygenase, and Kunitz trypsin inhibitor (KTI) proteins that can be allergenic and digestive inhibitors and reduce processing aptitude. Genetic removal of these four proteins is necessary in soybean breeding. Therefore, this study was conducted to select a new line with brown seed coat, green cotyledon, and tetra-null genotype (lecgy1lox1lox2lox3ti) for lectin, 7S α′ subunit, lipoxygenase, and KTI proteins in the mature seed. Five germplasms were used to create breeding population. From a total of 58 F₂ plants, F₂ plants with lele genotype were selected using a DNA marker, and F₃ seeds with a brown seed coat, green cotyledon, and the absence of 7S α′ subunit protein were selected. Three lines (S1, S2, and S3) were developed. Genetic absence of lectin, 7S α′ subunit, lipoxygenase, and KTI proteins was confirmed in F₆ seeds of the three lines, which had a brown seed coat, green cotyledons, and a white hilum. The 100 seed weights of the three lines were 26.4-30.9 g, which were lower than 36 g of the check cultivar - 'Chungja#3'. The new S2 line with 30.9 g hundred seed weight can be used as a parent to improve colored soybean cultivars without antinutritional factors such as lectin, 7S α′ subunit, lipoxygenase, and KTI proteins.

• Applied Biological Chemistry
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• v.42 no.4
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• pp.304-309
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• 1999

Two Lectins, designated FVL-1 and FVL-2, were isolated and purified from the fruiting bodies of edible mushroom Flammulina veluripes using ammonium sulfate fractionation, ethanol treatment, DEAE-TOYPEARL ion-exchange column chromatography, and TSK-Gel HW-55F column chromatography. Specific activity increased 18 folds for FVL-1 and 7.9 folds for FVL-2 from ethanol treated sample. SDS-PAGE of FVL-1 and FVL-2 gave apparent molecular mass of 10.6 kDa and 37 kDa, respectively. FVL-2 agglutinated all type of human erythrocytes (A, B, AB, and O). However, FVL-1 agglutinated more human erythrocyte type O than type A, B, and AB. The hemagglutination activities of the FVL-1 were effectively inhibited by bovine submaxillary and porcine stomach mucins(BSM and PSM), fetuin, asialofetuin and cations, such as $Cu^{2+}$, $Mg^{2+}$, $Ca^{2+}$, $Mn^{2+}$ and $Fe^{2+}$. However, FVL-2 was not inhibited by any cations. The hemagglutination activities of the two lectins were not inhibited by the sugar, such as lactose, galactose and sugar derivatives. FVL-1 and FVL-2 were stable at pH $5{\sim}11$ and pH $4{\sim}7$, respectively. FVL-1 was stable below $55^{\circ}C$ and FVL-2 was below $45^{\circ}C$.

• YAKHAK HOEJI
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• v.51 no.4
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• pp.259-263
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• 2007

We previously reported the isolation of a sialic acid-specific lectin eluted from the bark of Maackia fauriei using alkaline buffer on a fetuin-affinity column. Application of a borate-based elution buffer in the present study increased the specific activity of purified lectin from crude protein extract by 2.6-fold, whilst only slightly decreasing the recovery by 1.13%. The biological properties of the lectin eluted with borate buffer were the same as those of the lectin eluted with alkaline buffer such as in terms of the hemagglutination activity, hemagglutination inhibition activity, molecular mass, purity, and cytotoxicity to human breast cancer cells. A prepared biotin-labeled lectin conjugate was used to investigate the binding to various glycoproteins. Our results indicate that eluting with borate buffer is more efficient than using alkaline buffer to isolate the lectin adsorbed in a fetuin-affinity column.

• Proceedings of the Korean Environmental Sciences Society Conference
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• 2002.05b
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• pp.475-476
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• 2002

$SO_2$ 폭로군의 기관 상피층의 섬모에서 DBA 및 SBA는 50ppm 이하 $SO_2$ 폭로군에서는 대조군에 비해 증가하였으며 sWGA 및 UEA-1은 대부분의 $SO_2$ 폭로군에서 대조군에 비해 증가하였다. 섬모세포에서 LCA 및 Con A는 100ppm 및 200ppm $SO_2$ 폭로군에서 대조군에 비해 약간 증가하였다. 배상세포에서는 대부분의 렉틴의 반응성이 50ppm 이하의 $SO_2$ 폭로군에서는 증가하였다가 100ppm 및 200 ppm $SO_2$ 폭로군에서는 현저히 감소하였다. 장액선포에서는 LCA 및 Con A는 모든 $SO_2$ 폭로군에서 대조군보다 증가하는 경향을 보였으며 점액선포에서는 대조군에서 관찰되지 않았던 RCA-1은 50ppm 및 100ppm $SO_2$ 폭로군의 일부 선포에서 증가하였다. 위의 결과로 보아 $SO_2$는 기관에 심대한 병리조직학적 변화뿐만 아니라 glycoconjugates대사에 심대한 영향을 미쳐 심한 병변을 야기시킴을 알 수 있었다. 전반적으로 $SO_2$의 호흡기 영향은 고농도로 갈수록 심한 영향을 나타내었다. 저농도에서도 폭로 시간이 길어짐에 따라 나타나는 $SO_2$의 영향이 고농도와 유사한 경향을 나타내며 또한 모든 $SO_2$의 농도를 비교해보면 폭로 시간이 길어질수록 그 영향이 더 심하게 나타났다.

• Korean Journal of Food Science and Technology
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• v.43 no.1
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• pp.72-76
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• 2011

The adjuvant effects of Korean mistletoe lectin-C (KML-C) were investigated following the oral administration of KML-C with ovalbumin (OVA) as an antigen. Mice were orally immunized with OVA alone or admixed with various doses of KML-C or cholera toxin (CT), and the titer of OVA-specific antibody in the serum and mucosal secretions were determined. OVA+KML-C-treated mice showed high titers of IgA specific to CT in mucosal secretions. The antibody titers in the serum of OVA+KML-C-treated mice were comparable to those in the serum of OVA+CT-treated mice. When mice were immunized with OVA+KML-C or with CT alone and subsequently injected with OVA on the footpads after the primary immunization, they showed a more significant increase in delayed-type hypersensitivity reactions than when they were administered CT alone. These results suggest that KML-C is a potent immunoadjuvant that enhances both humoral and cellular immunity by the mucosal immune system.

• YAKHAK HOEJI
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• v.53 no.1
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• pp.34-40
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• 2009

The glycosylation of therapeutic glycoproteins can affect their efficacy, stability, solubility, and half-life. Analyzing the composition of monosaccharides, such as that of neutral and amino sugars, is the first step for elucidating the structure of glycan attached to glycoproteins. In the present study, neutral and amino sugars of lectin obtained from Maackia fauriei were analyzed using an enzyme-linked lectinsorbent assay (ELLA) and high-performance anion exchange chromatography with pulsed amperometric detection (HPAEC-PAD). Peroxidase-labeled lectins such as concanavalin A, Ricinus communis agglutinin, and soybean agglutinin were used for ELLA, since they specifically bind to the monosaccharide residue most frequently encountered in a glycan. The hydrosylate of lectin was prepared by treatment with trifluoroacetic acid, which resulted in the lectin mainly possessing the N-glycan consisting of 98.1 pmol Fuc, 342.1 pmol GlcN, 51.9 pmol Gal, 678.9 pmol Man, and 330.7 pmol Xyl. The present results demonstrate that ELLA and HPAEC-PAD are very effective methods for rapidly estimating the types and relative amounts of monosaccharides in intact glycoproteins.