• Title/Summary/Keyword: lectin

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Biochemical Properties of Seed Lectin from Korean Soybean Cultivars Developed for Soy Source (한국산 장류콩 종자 렉틴의 생화학적 특성)

  • Wang, Yushan;Roh, Kwang-Soo
    • KSBB Journal
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    • v.24 no.2
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    • pp.170-176
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    • 2009
  • Lectin was finally isolated on Sephadex G-100 from Korean soybean cultivars developed for soy source and investigated its some biochemical properties. Native PAGE pattern of this lectin revealed a molecular weight of 108 kDa as tetramer. The molecular weight of this lectin isolated as double protein band by SDS-PAGE was calculated to be 32 and 22 kDa from the relative mobilities compared with those of the standard proteins. Among the tested red blood cell, the isolated lectin agglutinated rabbit red blood cell treated with trypsin, but did not agglutinated human red blood cells (A, B, AB, O), rat, and untreated rabbit red blood cell. The optimal temperature and thermal stability of isolated lectin was at 20-$50^{\circ}C$ and 10-$60^{\circ}C$, respectively. This lectin was stable at 7.2, and showed complete loss in its activity below pH 6.2 and above pH 8.0.

Concentration and Immunological Characteristics of Lectin in Soybean (Glycine max L.) Cultivars (대두품종의 렉틴 함량과 면역학적 특성)

  • 박원목;김성환;윤경은
    • KOREAN JOURNAL OF CROP SCIENCE
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    • v.34 no.4
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    • pp.345-352
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    • 1989
  • The immunochemical property of lectin in soybean and the presence of lectin in seeds of six soybean cultivars were investigated by immunochemical methods. All seeds of six soybean cultivars formed one precipitin line against the soybean lectin antibody and showed immunochemically homologous precipitin pattern among the cultivars in immunodouble diffusion test. Four antigenic components in soybean lectin were detected by the crossed imuno-electrophoresis of a soybean seed antigen against the soybean lectin antibody. Cultivar, Jangyeop-kong contained the highest amount of lectin and the next were Kwangkyo, Hwangkeumkong, Baegunkong, and Jangbaegkong or Paldal-kong in order of lectin content. The lectin purified from the seeds of six soybean cultivars agglutinated rabbit erythrocytes, but did not agglutinate the fungal spores which were Fusarium sp., Alternaria sp., Cuvalaria sp., and Colletotrichum sp. isolated from the infected seeds or leaves of soybean.

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The Cytotoxicity of Rat Hepatocytes on Viscum album Lectin (겨우살이 lectin의 흰쥐 간세포 독성에 미치는 영향)

  • Chang, Choul-Soo;Ryu, Jae-Ki;Kim, Tae-Ho
    • Korean Journal of Clinical Laboratory Science
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    • v.39 no.3
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    • pp.190-195
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    • 2007
  • In the present study, the author investigated to the cytotoxocity in cultured rat hepatocytes of Viscum album lectin. The cytotoxcity effect in Viscum album lectin on the activity of LDH was also investigated. Viscum album lectin significantly increased LDH leakage into medium of hepatocytes treated or untreated with $CCl_4$ (p<0.001). However, Viscum album lectin significantly increased LDH leakage from $CCl_4$-induced hepatocyte (p<0.001). There was a significant increase in LDH levels relative to the control group. Histological observation basically supported the result obtained from LDH assay. The livers of rats challenged with $CCl_4$ produced a marked increased cytoplasmic vacuoles and inflammatory cells in number, while the number of necrotic cells and swollen hepatocytes did not change significnatly. Rats administered DMSO alone did not alter the normal hepatic architecture. Histological observation of liver section in rat treated 72 hrs with either Viscum album lectin $CCl_4$-induced liver damage showed number of cytoplasmic vaculoe and necrotic cell. The number of inflammatory cell increased markedly. This results suggest to the conclusion that Viscum album lectin has a effect of hepatotoxicity activator.

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Isolation and Characterization of Lectins from Stem and Leaves of Korean Mistletoe (Viscum album var. coloratum) by Affinity Chromatography

  • Park, Won-Bong;Han, Seon-Kyu;Lee, Myung-Hwang;Han, Kwang-Ho
    • 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.

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Biochemical Properties of Locular Fluid Lectin of Tomato (토마토 Locular Fluid Lectin의 생화학적 성질)

  • Roh, Kwang-Soo
    • 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.

Changes of Lectin from Viscum coloratum by Fermentation with Lactobacillus plantarum -Isolation and Purification- (유산균 발효에 의한 겨우사리 중의 렉틴 성분의 변화 -분리 및 정제-)

  • Park, Won-Bong;Kim, Hee-Sook
    • YAKHAK HOEJI
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    • v.38 no.6
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    • pp.687-695
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    • 1994
  • Lectin from mistletoe(Viscum coloratum) fermented by Lactobacillus plantarum for 1,2,3 days were obtained by salt fractionation, gel filtration, anion exchange chromatography and SDS-PAGE, and compared with the lectin from unfermented mistletoe. The new lectin of molecular weight of about 18,500D from fermented mistletoe was identified.

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The Effect of Root Exudate and Chemotaxis on Host Recognition in Soybean-Bradyrhizobium Symbiosis (대두(大豆)-근류균(根瘤菌) 공생(共生)에서 뿌리분비물(分泌物)과 화학주성(化學走性)이 숙주인식(宿主認識)에 미치는 영향(影響))

  • Kang, Sang Jai;Park, Woo Churl
    • Current Research on Agriculture and Life Sciences
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    • v.11
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    • pp.121-132
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    • 1993
  • This study was carried out to research the effect of the chemotaxis of Bradyrhizobium japonicum KCTC 2422 and its mutant toward soybean root exudate and to elucidate the effect of the lectin of host specificity (Host Recognition) in soybean-Bradyrhizobium symbiosis. The results obtained were as follows: The homogeneities of the purified lectins from soybean and pea seed was ascertained chromatographically and electrophoretically. Gel electrophoresis of soybean lectin in the presence of sodium dodecyl sulfate appeared a single protein band, whereas pea lectin appeared two protein bands. Soybean lectin from 2 cultivars formed immunoprecipitin arcs at same position with anti-soybean lectin rabbit IgG, but pea lectin did not form immunoprecipitin lines with anti-soybean lectin rabbit IgG. Chemotactic responses of KCTC 2422, LPN-100 and LCR-101 toward proline in capillary assays were 3.1, 1.3 and 1.0-fold above background, respectively. The chemotactic responses of KCTC 2422, LPN-100, and LCR-101 toward Paldal crude root exudate in capillary assays were 3.5, 1.4 and 1.4-fold above background, respectively. The present work shows that B. japonicum and its mutants are capable of very different responses toward root exudate fraction. The chemotactic responses of KCTC 2422 was most with neutral fraction, least with anionic fraction and intermediate with cationic fraction. The nitrogenase activity of soybean nodule was shown in 15days after inoculation with LCR-101. However, we couldn't find out the nodules when soybean was inoculated with LPN-100. From these result we can suppose that the chemotaxis of Bradyrhizobium plays inportant the role of forming the nodule (host recognition) in the soybean-B. japonicum symbiosis.

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Purification Efficiency of a Lectin from Maackia fauriei (솔비나무 유래 렉틴의 정제 효율)

  • Bae, Chan-Hyung;Kim, Ju-Cheol;Kim, Yu-Jeong;Kim, Sang-Gu;Na, Kwang-Heum;Park, Byung-Tae;Kim, Ha-Hyung
    • 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.

Effect of Lipid Metabolism in Viscum album Lectin on Rats (겨우살이 Lectin이 지질대사에 미치는 영향)

  • Chang, Choul Soo;Hwang, Seock Yeon
    • Korean Journal of Clinical Laboratory Science
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    • v.36 no.2
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    • pp.131-136
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    • 2004
  • This study was carried out to investigate effect of lipid metabolism in Viscum album lectin on rats. The lectin was purified by sepharose 4B affinity chromatography and gel filtration using sephadex G-150 with plant material from Viscum album collected in Mt. Duk Yui. After 72 h of $CCl_4$ injection (in olive oil, 1:1, 2 mg/kg) there was a significant increase in serum total cholesterol and triglycerige levels relative to the control group. However, treatment of both Viscum album and purified lectin were significantly decreased lipid parameters against the $CCl_4$-induced. Histological observation basically supported the result obtained from serum lipid assay. The livers of rats challenged with $CCl_4$ produced a marked increase of cytoplasmic vacuoles in number, while the number of necrotic cells and swollen hepatocytes did not change significnatly. Rats administered olive oil alone did not alter the normal hepatic architecture. Histological observation of the liver section in rats treated 72 h with either Viscum album purified lectin or $CCl_4$-induced liver lipogenesis showed decreased numbers of cytoplasmic vaculoes and necrotic cells. The normal hepatic architectural pattern was observed in Hematoxylin-eosin stain. These results suggest that Viscum album lectin has a possible protective effect of lipid metabolim in rats.

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Antifungal Activity and Biochemical Characterization of Lectin Isolated from Locular Fluid of Cherry Tomato Fruit (방울토마토 열매 locular fluid lectin의 항균성과 생화학적 특성)

  • Roh, Kwang-Soo
    • KSBB Journal
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    • v.25 no.3
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    • pp.289-296
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    • 2010
  • Lectins are carbohydrate-binding and a cell-agglutinating proteins, and are concerted with a plants defence mechanism. In particular, chitin-binding lectins in locular fluid of cherry tomato fruit seemed to have a role in defending plants against fungi. The antifungal activity using lectin isolated from locular fluid of cherry tomato fruit was measured in the plant pathogen Cladosporium cucumerinum, Monosporascus cannonballus, Fusarium oxysporum, and Rhizoctonia solani. Amoung the four strains, a potent antifungal activity was detected in Cladosporium cucumerinum and Monosporascus cannonballus, not in Fusarium oxysporum, and Rhizoctonia solani. The molecular weight of this lectin isolated as double protein bands by SDS-PAGE was calculated to be 87 kDa and 47 kDa from the relative mobilities compared with those of reference molecular weight markers. The isolated lectin agglutinated human red blood cells (A, B, AB, O) treated with trypsin, and the most activity was found at B. The optimal temperature of isolated lectin was at $30^{\circ}C$. For the thermal stability, lectin was stable at $20-80^{\circ}C$. The optimal pH of this lectin was at 7.2, and showed complete loss below pH 9.0.