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

• YAKHAK HOEJI
• /
• v.37 no.3
• /
• pp.254-261
• /
• 1993

Developing new substance for immunosuppressor or immunomodulator from natural products is extremely important in the present biomedicine. In this paper, we focused our efforts on the mitogenicity and immunochemical properties of the two lectins (LCC-I, LCC-II) obtained from marine animal Lunella coronata coreensis. Immunochemical techniques were employed to elucidate the structural and/or functional similarities between the LCC lectins. Molecular weight of the LCC lectins, LCC-I and LCC-II were estimated to be around 60 KD and 66-70 KD, respectively. LCC lectins were mitogens for murine splenic lymphocytes, and the optimum mitogenic doses were 31.25 $\mu\textrm{g}$/ml and 3.91 $\mu\textrm{g}$/ml, respectively. LCC-II lectin was a good mitogen toward human peripheral lymphocytes at a concentration about 31.25 $\mu\textrm{g}$/ml.

• YAKHAK HOEJI
• /
• v.36 no.3
• /
• pp.241-249
• /
• 1992

The whole body extract of Lunella coronata coreensis agglutinated nonspecifically human and other animal erythrocytes. A new lectin was purified by the following procedures: 0.15 M NaCl extraction, salt fractionation, gel filtration, anionic and cationic ion exchange column chromatographies. Through these purification procedures, specific activity of LCC-I was increased from 276 to 9714.3 units/mg, And on polyacrylamide gel electrophoresis, LCC-I exhibited one major band. A molecular weight of LCC-I was assumed to be 20,000 by sodium dodesyl sulfate polyacrylamide gel electrophoresis. The purified lectin was relatively stable at various pH and heat. Among the tested sugars, lactose and lactulose inhibited lectin activity at a concentration of 6.25 mM, respectively.

• Korean Journal of Pharmacognosy
• /
• v.25 no.2
• /
• pp.121-131
• /
• 1994

Two kinds of new lectins, CATL-I and CATL-II, were partially purified from the intestine of Chlorostoma argyrostoma turbunatum by physical saline extraction, salt fractionation, ion exchange chromatography and gel filtration. CATL-I and CATL-II were purified 39.4 and 15.8 fold with a yield of 8.8 and 7.4%, respectively. On polyacrylamide gel electrophoresis, CATL-I demonstrated one major and one minor bands. This lectin agglutinated human and other animal erythrocytes nonspecifically and also agglutinated murine splenic lymphocytes. Carbohydrate specificity of the lectins was determined by inhibition of the agglutinability by methyl-${\alpha}-_D$-galactopyranoside and $_L-rhamnose$ at a final concentration of 6 mM. The lectins contained relatively high amounts of acidic amino acids, but the contents of sulfur containing amino acids were very low or was not estimated. Immunochemical studies were carried out to identify some properties of marine animal lectins.

• Korean Journal of Pharmacognosy
• /
• v.42 no.1
• /
• pp.68-75
• /
• 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
• /
• v.45 no.3
• /
• pp.251-257
• /
• 2001

The study was carried out to evaluate the preliminary toxicity and general pharmacology of KML-IIU, a purified pectin from Korean Mistletoe (Viscum album coloratum). KML-IIU was administered intravenously to ICR mice and Spargue-Dawley rats to investigate the acute toxicity. LD50 values in mice and rats were above 30 $\mu$g/kg. KML-IIU had no effects on the general behaviors, acetic acid induced writhing syndrome, pentobarbial induced sleeping time, pentylenetetrazole induced convulsion and the change of body temperature. In addition, KML-IIU did not show any effects on digestive system and blood coagulation system.

• YAKHAK HOEJI
• /
• v.39 no.3
• /
• pp.252-259
• /
• 1995

Isolation, purification and characterization of biophysicochemical properties of the three new lectins, MLA-I, MLA-II, MLA-III from the hemolymph of Meretrix lusoria have been reported previously. A series of immunochemical studies were investigated in this work. The three lectins were revealed as having partial identity each other by immunodiffusim and immunoelectrophoresis. These results suggest that MLA lectins are isolectins having similar biophysicochemical properties. Particularly, MLA-I proved to be a potent mitogen for murine splenic as well as human peripheral lymphocytes, and the optimum mitogenic dose were 62.5 and 1.95 $\mu\textrm{g}$/ml, respectively.

• YAKHAK HOEJI
• /
• v.46 no.4
• /
• pp.270-275
• /
• 2002

The lectin gene from rice was amplified by the polymerase chain reaction. The amplified DNA was inserted into the expression vector pET26b and expressed it as a fusion protein with polyhistidine sequences in Escherichia coli. The recombinant protein was produced by induction with 0.4 mM isopropyl-$\beta$-D-thiogalactopyranoside at 37$^{\circ}C$ and purified by an immobilized metal affinity chromatography. The recombinant protein was found to have lectin activity by the hemagglutination inhibition assay. The hemagglutination activity of the recombinant protein was optimal at pH 4.0-7.0 and was dependent on $Ca^{2+}$ and Mn$^{2+}$.2+/.

• YAKHAK HOEJI
• /
• v.39 no.3
• /
• pp.260-267
• /
• 1995

A lectin from the edible mushroom, Lentinus edodes, was purified through physiological saline extraction, ammonium sulfate fractionation and column chromatographies. On polyacrylamide gel electrophoresis, 0.05M fraction from hydroxyapatite column exhibited adjacent four sharp bands. The partially purified lectin agglutinated the erythrocytes of rabbit, mouse and rat, but not agglutinated human erythrocytes. The lectin's mitogenic effects were tested by its application to human and murine splenic lymphocytes. The results showed that the 0.05M fraction from hydroxyapatite was mitogenic, and the optimal dose of Lentinus edodes lectin was slightly lower than Con A by the culture with murine splenic and human peripheral lymphocytes. Meanwhile, its ability to agglutinate transformed cells was tested by its administration to continuous cell lines L1210 and HeLa cells. The leetin was found to be an agglutinin of tumor cell lines tested by L1210 and HeLa cells.

• YAKHAK HOEJI
• /
• v.39 no.3
• /
• pp.243-251
• /
• 1995

Three new lectins, MLA-I, MLA-II and MLA-III, have been isolatedand purified from the hemolymph of Meretrix lusoria and reported previously. Biophysicochemical characteristics were investigated with these three MLA lectins. The MLA lectins agglutinated human erythrocytes non specifically and proved as D-galactose group carbohydrate specific. Molecular weight of ML.A-I. II and III were estimated to be 330, 500 and 310KD, respectively, by gel filtration on Sepharose CL-6B column. On SDS-polyacrylamide gel electrophoresis, ML.A-I was dissociated into a single subunit of 42KD, MLA-II was into the twelve subunits of 46, 32, 30, 28, 25, 23. 22, 20. 19, 16, 15, and 14KD, and MLA-III was into the two subunits of 72 and 44KD. The pl of MLA-I, II, III were 4.0. 4.9 and 5.0. Amino acid analysis revealed a high contents of acidic and hydroxy amino acids, and a paucity of sulfur containing amino acids. Proline was not contained in MLA-II.