• BMB Reports
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• v.28 no.1
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• pp.6-11
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• 1995

A new lectin, named TRA, was purified from Trichosanthes kirilowii root by acid-treated Sepharose 6B, Mono-Q, and TSK-gel 3000SW column sequential chromatography. The lectin appeared homogeneous by native gel electrophoresis at pH 4.3 and gave two protein bands of Mr=31 and 28 kDa by SDS-PAGE. The N-terminal amino acid sequences of the polypeptides of TRA have not been reported in amino acid sequences of the lectins. TRA lectin formed a precipitate with asialofetuin, neuraminidase-treated fetuin. A sugar inhibition assay indicated that N-acetyl-D-galactosamine, among the monosaccharides tested, was the most potent inhibitor of TRA-induced hemagglutination. Asialofetuin showed a 260-times stronger inhibitory activity than N-acetyl-D-galactosamine. TRA lectin also showed agglutination with normal leukocytes and lymphoma cells, but not with premature hemopoietic cells. These results suggest that TRA is a novel plant lectin.

• YAKHAK HOEJI
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• v.54 no.6
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• pp.449-454
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• 2010

The glycosylation of glycoproteins from mammalian or plants can affect their efficacy, stability, solubility, and half-life. In the present study, we investigated plant glycosylation and their relative intensity (%) in a plant carbohydratebinding protein with the hemagglutination and antiproliferative activities. The hemagglutination activity on the deglycosylated protein was decreased as a 16-fold than that of intact glycoprotein. Using the HPLC with fluorescence detector and mass spectrometer, the major eight bi- or triantennary oligosaccharides containing xylose, fucose, mannose, galactose, and N-acetylglucosamine were identified and structurally characterized. The present results indicate that the oligosaccharides on this plant glycoprotein is necessary for their own property.

• Korean Journal of Veterinary Service
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• v.40 no.3
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• pp.187-192
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• 2017

In this report, fifteen monoclonal antibodies (MAbs) against an avian influenza virus (H9N2 subtype) were newly produced and characterized. These MAbs proved to react to the epitopes of nucleocapsid protein (NP), hemagglutinin (HA), neuraminidase (NA) and non-structural protein 1 (NS1) of Korean H9N2 strain, respectively. Two HA-specific MAbs showed the ability to inhibit the hemagglutination activity of H9N2 subtype avian influenza virus when tested by hemagglutination inhibition (HI) assay. All MAbs did not cross-react with other avian-origin viruses (Newcastle disease virus, infectious bursal disease virus, infectious bronchitis virus and avian rotavirus) by immunofluorescence test or enzyme-linked immunosorbent assay. The MAbs produced in this study could be useful as the materials for diagnostics and therapeutics against Korean-lineage H9N2 virus infections.

• YAKHAK HOEJI
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• v.40 no.2
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• pp.202-211
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• 1996

Experiments were performed on male Sprague-Dawley rats to investigate the immunobiological effects on route of administration of amygdalin(AM). Rats were administered orally at 12.5, 25, or 50mg/kg/day of AM or injected wtih 25,50, or 100mg/kg/day of AM intravenously for 2 weeks. Rats were immunized and challenged with sheep red blood cells(SRBC). The results of this study were summarized as follows;(1) In oral administration of AM, body weight gains were significantly increased by 50mg/kg AM as compared with controls, the relative weights of liver and thymus also were significantly increased by 12.5 and 25mg/kg AM. However, 2-mercaptoethanol-resistant hemagglutination titier (2-MER HA), Plaque forming cells (PFC) and rosette forming cells (RFC) were non-dose dependently decreased. Phagocytic activity and delayed-type hypersensitivity (DTH) reaction also were significantly decreased by 50mg/kg AM. (2) In intravenous injection of AM, body weight gains, hemagglutination titer (HA), 2MER-HA, DTH reaction, PFC, RFC and circulating leukocytes were not influenced by AM. However, the relative weights of liver, spleen and thymus were significantly enhanced 100mg/kg AM. These results indicated that oral administration of AM non-dose dependently suppresses humoral and cell-mediated immunity in SD rats, and that intravenous injection of AM is unaffected humoral and cell-mediated immunity, however, the high dose of it significantly enhances phagocytic activity.

• YAKHAK HOEJI
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• v.36 no.4
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• pp.291-302
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• 1992

Effects of Zinc chloride on the immune responses were studied in ICR mice. ICR male mice were divided into 5 groups(10 mice/group) and Zinc chloride at doses of 0.3, 1.2, 4.8 and 19.2 mg/kg were orally administered to ICR male mice once a day for three weeks. Mice were sensitized and challenged with sheep red blood cells(S-RBC). The results of this study were summarized as follows; (1) Zinc chloride significantly increased the body weight rate, the weight ratios of spleen and thymus to body weight and the number of circulating leukocyte, but significantly decreased them at the high dose of it, and increased dose-dependently the weight ratio of liver to body weight. (2) Zinc chloride significantly increased hemagglutination titer, Arthus reaction and plaque forming cell related to humoral immunity, but significantly decreased them at the high dose of it. (3) Zinc chloride significantly increased delayed-type hypersensitivity reaction and rosette forming cell related to cellular immunity, but significantly decreased them at the high dose of it. (4) Zinc choride significantly enhanced phagocytic activity, but significantly decreased according to the increase of its dose. These results suggest that high dose of zinc chloride decreased humoral, cellular and non-specific immune responses.

• Food Science and Biotechnology
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• v.15 no.1
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• pp.91-95
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• 2006

Effects of cultivars, cooking, and processing on hemagglutinin activity were evaluated by observing macroscopic hemagglutination using serial twofold dilution of trypsinized human blood type-O or rabbit blood. Hemagglutinin activity was expressed as maximal geometric dilution fold. Agglutination of rabbit blood was more sensitive compared to human blood. Hemagglutinin activities of glyphosate-tolerant soybean, HS2906, and imported conventional soybeans were not statistically different, although significant differences were observed among conventional soybean cultivars cultivated in Korea (286 to 1535 HU/mg protein). Time required to reach fifty percent inhibition of hemagglutinin activity ($IT_{50}$) value decreased with increasing cooking temperature and pressure. Most effective conventional cooking method to inhibit hemagglutinin activity was pressure-cooking ($IT_{50}$: 1.36 min). Calculated activation energy based on reaction rate constant was 4.88 kcal. No hemagglutinin activities were detected in processed soybean products such as tofu, soybean paste, and soysauce.

• YAKHAK HOEJI
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• v.38 no.4
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• pp.418-424
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• 1994

Lectin from mistletoe (Viscum coloratum) were obtained by salt fractionation, gel filtration and anion exchange chromatography. A molecular weight of about 60,000D has been determined by SDS-PAGE and two basic subunits which have molecular weights of 33,000D and 28,000D are linked by a disulfide bond. The partially purified mistletoe lectins agglutinated human B erythrocytes. Agglutinating activity was relatively stable at varied pH $(3.77{\sim}8.71)$ and at temperature range of $0{\sim}40^{\circ}C$ and not affected by 9 metal ions. Galactose, lactose and N-acetyl-D- galactosamine inhibited agglutinating activity of lectin. Lectin from mistletoe was more mitogenic to murine lymphocytes than concanavalin A.

• Journal of Veterinary Clinics
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• v.14 no.2
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• pp.268-272
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• 1997

This study was performed to estimate the clinical signs and biochemical para meters of indicator on acute hepatic injury induced by the administration of CCl$_{4}$ in rats. Minor behavioral changer brittleness of skin hair and decreased volume of water and food intake were observed in rats after 2 hours of $CCl_{4}$ administration compared to control group. Concentration of serum albumin has shown lower than that of control group. However concentration of total bilirubin has shown higher than that of control group. As times go onto serum LDH activity was significantly increased compared to control Broup. Serum CPK activity hasn't shown change compared to control group. Passive hemagglutination that of afetoprotein was shown negative reaction in all the treatment groups and control group.

• Archives of Pharmacal Research
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• v.20 no.4
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• pp.306-312
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• 1997

We attempted to isolate and characterize the lectins from stem and leaves of Korean mistletoe (Viscum album var. coloratum) by affinity chromatography. Lectin I was isolated only from stem. Lectin II was not isolated from Korean mistletoe, whereas lectin III was isolated from the stem and leaves. The hemagglutinating activity of lectin I was 16HU and inhibited by D-galactose, lactose, and N-acetyl-D-galactosamine. The lectin I has molecular weight of 60, 000D being composed of two basic subunits with molecular weights of 32, 000D and 28, 000D which are linked by a disufide bond. The lectin III from stem has molecular weight of 66, 000D being two basic subunits which have molecular weights of 34, 000D and 29, 000D and are linked by a disufide bond. The activity of lectin I was stable at the pH range of 4.00-8.50 and at a wide range of temperature (0-42.deg. C). The lectin I showed more potent mitogenic activity to murine lymphocytes than concanavalin A.

• KSBB Journal
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• v.23 no.1
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• pp.48-53
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• 2008

Lectin was isolated from locular fluid of tomato by affinity chromatography using Sephadex G-200, and studied its some biochemical properties. SDS-PAGE of the isolated lectin revealed a tetramer composed of two identical subunits with molecular weights of 39 and 23 kDa. The isolated lectin was agglutinated by trypsin-treated human ABO type blood erythrocytes with similar potency, and the most activity of agglutination was found at B type blood erythrocyte. This lectin showed maximum thermal stability at $70^{\circ}C$, and was relatively stable to heat with the higher activity at $40-80^{\circ}C$. The optimal temperature and pH of this lectin were $50^{\circ}C$ and pH 7.0, respectively.