• Title, Summary, Keyword: Lectin

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Binding Affinity between Lectin and Rhizobia in Soybean-Bradyrhizobium Symbiosis (대두-근류균의 공생에서 Lectin에 의한 결합특이성)

  • Kim, Jin-Ho;Park, Woo-Churl;Kang, Sang-Jae
    • Applied Biological Chemistry
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    • v.40 no.6
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    • pp.546-550
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    • 1997
  • This study was carried out to elucidate the biological characteristics of Rhizobia in biological nitrogen fixation system. The results of investigation were as follows; Polyacrylamide gel electrophoresis pattern of root lectin in the presence of SDS was ascertained electrophoretically and chromatographically. The purified root lectin formed immunoprecipitin line with anti lectin rabbit IgG. Root lectin, seed lectin and root exudate were tested for chemotactic ability. Chemotactic responses of RCR3407 and KCTC2422 toward root exudate were stronger than those of seed lectin and root lectin, but there didn't occur chemotactic responses of LPN100, not bound with seed lectin and that of LPN101, bound with seed lectin toward root exudate, root lectin and seed lectin. RCR3407, KCTC2422 and LPN-101, which nodulated with soybean, interacted with soybean lectin, but not with pea lectin. LPN-100, which was not nodulated with soybean, didn't interact with soybean lectin.

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Expression of Recombinant Korean Mistletoe(KM) Lectin and B genes in Saccharomyces cerevisiae (Saccharomyces cerevisae에서 한국산 겨우살이 유래 lectin A 및 B 유전자의 발현)

  • 최윤혁;김종배;양웅석;황철원
    • Journal of Life Science
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    • v.14 no.5
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    • pp.840-846
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    • 2004
  • A study for expression of Korean Mistletoe (KM) lectin gene (A,B) in Saccharomyces cerevisiae was done using transforming system of yeast. In order to overexpress the genes efficiently in yeast, two lectin genes (A,B) were re-cloned and modified including Kozak translation initiation sequence using PCR amplification. The constructed plasmids containing modified lectin A and B genes were transformed to S. cerevisea INVSc (MAT G, his3 $\Delta$1, leu2, trpl-289, ura3-52). The transformed cells were identified by DNA sequencing with ABI3700 system and induced with 2% of galactose for recombinant KM lectin (rKM lectin) protein. The rKM lectin A and B proteins were determinated about 29kDa size of protein by SOS-P AGE and western blotting analysis. The expressed recombinant lectin was determinated 1.24∼1.75 $\mu\textrm{g}$ per 1 mg of cytosolic soluble protein by sandwich ELISA method. Moreover the lectin genes were expressed as maximum level at 36 h after galactose induction and lectin A gene was were repressed after 48 h.

Biochemical Characterization of Lectin Purified from Kidney Bean Seedling (강낭콩 유식물로부터 분리한 Lectin의 생화학적 특성)

  • Roh, Kwang-Soo
    • KSBB Journal
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    • v.22 no.1
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    • pp.53-57
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    • 2007
  • We have studied biochemical characterization of lectin purified from kidney bean seedling through PBS extraction, $(NH_4)_2SO_4$ precipitation, and Sephadex G-100 affinity chromatography. The lectin was agglutinated by rabbit erythrocytes. This lectin analyzed by SDS-PAGE is a tetramer composed of two subunits with molecular weights of 46 and 44 kDa. The optimal temperature and thermal stability of the lectin was 30$^{\circ}C$ and 40-80$^{\circ}C$, respectively. The maximal pH of this lectin was pH 8.2.

Anti-diabetic Effect of Viscum album Lectin (겨우살이 Lectin의 항당뇨 효과)

  • 장철수;노광수
    • Biomedical Science Letters
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    • v.6 no.2
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    • pp.151-157
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    • 2000
  • We investigated anti-diabetic effect of the crude extracts and lectin purified from the leaves of Viscum album collected in Mt. Duk Yu. The induction of diabetes mellitus was confirmed by the presence of statistically significant greater serum glucose levels in strptozotocin-treated rats compared with the untreated non-diabetic group. There are no significant differences in the serum glucose levels compared extracts and purified lectin to tap water in the non-diabetic group after administration through the oral cavity in 29 day. But for streptozotocin-induced diabetic rats the serum glucose level in extracts after administration through the oral cavity was strikely decreased to 36% than tap water in 29 day. Significantly lower glucose level was obtained at 2 hr and 4 hr after administration of purified lectin(0.4 mg/kg) through the peritoneal cavity. These results provide an evidence that Viscum album lectin has an andti-diabetic effect pharmacologically.

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Effects of Lectin-conjugated Ellagitannin on Inhibition of Melanoma Metastasis (Lectin-conjugated Ellagitannin의 흑색종에 대한 전이억제효과)

  • Kim, Hyoung-Kun;Han, Ki-Sook;Lee, Do-Ik
    • YAKHAK HOEJI
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    • v.44 no.6
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    • pp.601-606
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    • 2000
  • Recently, studies on missile antitumor drugs, which selectively act on tumor cell and display drug effects, have been performed. These missile antitumor drugs which can increase drug effects and decrease side effects, are ideal medication method. Lectin has been reported as tumor cell specific binding protein and tannin as antitumor substance. In this study, we studied inhibition of melanoma metastasis by lectin-conjugated ellagitannin and used praecoxin A as ellagitannin source. Mouse melanoma cell, B16-F10, was injected into the sole of forefoot of C57BL/6 mouse, and after administration with drug, the number of pulmonary tumor colony was counted. The administration of praecoxin A, lectin-praecoxin A mixiture, and lectin-conjugated praecoxin A was started after amputation of established tumor foci at right forefoot of mice and continued for 3 weeks with i.p. injection of one of those drugs A every 24 hours. Lectin-praecoxin A mixture, and lectin-conjugated praecoxin A significantly reduced the number of spontaneous pulmonary metastasis. Exposure to 5 mg/kg of lectin-praecoxin A mixiture and lectin-conjugated praecoxin A produced a statistically significant 38.3%, 41.8% reduction in the number of remaining pulmonary metastasis. These results suggest that metastasis inhibition by lectin-praecoxin A mixiture and lectin-conjugated praecoxin A are better than that of praecoxin A.

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Molecular characterization of a lectin, BPL-4, from the marine green alga Bryopsis plumosa (Chlorophyta)

  • Han, Jong-Won;Yoon, Kang-Sup;Jung, Min-Gui;Chah, Kyong-Hwa;Kim, Gwang-Hoon
    • ALGAE
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    • v.27 no.1
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    • pp.55-62
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    • 2012
  • A novel lectin specific to N-acetyl-D-galactosamine as well as N-acetyl-D-glucosamine was isolated from Bryopsis plumosa and named as BPL-4. Sodium dodecyl sulfate polyacrylamide gel electrophorese (SDS-PAGE) and matrix-assisted laser desorption / ionization-time of flight (MALDI-TOF) mass spectrometry data showed that this lectin was a monomeric protein with molecular weight 12.9 kDa. The N-terminal amino acid sequences of the lectin were determined by Edman degradation and the full cDNA sequence encoding this lectin was obtained using the degenerate primers designed from the amino acid sequence. The size of the cDNA was 414 bp containing single open reading frame (ORF) encoding the lectin precursor. The homology analysis showed that this lectin might belong to H lectin group. BPL-4 showed high sequence similarity (60.6%) to BPL-3, which is a previously reported lectin from the same species. The comparative analysis on the lectin's primary structure showed two conserved domains including one possible active domain of H lectin group.

Biochemical Characteristics of Lectins Isolated from Lentinula edodes (표고버섯으로부터 분리한 렉틴의 생화학적 특성)

  • Kim, Young-Sin;Cho, Nam-Seok
    • Journal of the Korean Wood Science and Technology
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    • v.29 no.4
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    • pp.79-88
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    • 2001
  • Lectin was isolated from shiitake mushroom (Lentinula edodes) with 0.15 M NaCl solution, and purified by the following procedures : precipitation by ammonium sulfate, anion exchange column chromatography on DEAE Sephadex A-50 and hydroxyapatite column chromatography. The fresh pileus part of the mushroom contained more than two times of lectin compared to the stipe part, and lectins and its activity were reduced by heating. The extraction yield of crude lectin was 46.03%, 28% yield after purification on on DEAE Sephadex A-50 column chromatography. Some amino acids, aspartic acid, serine, alanine and histidine, were increased by purification process. Relatively low molecular weight parts of lectin had the agglutinating activity for rabbit blood, and its molecular weight was about 23 kDa The molecular weights of purified lectins, LA-a and LB-b, by the hydroxyapatite column chromatography were 24 kDa and 23 kDa, respectively.

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Effects of Lectin-conjugated Ellagitannin on Antitumor Activity (Lectin-conjugated Ellagitannin의 혹색종에 대한 항암활성)

  • Kim, Hyoung-Kun;Han, Ki-Sook;Lee, Do-Ik
    • YAKHAK HOEJI
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    • v.44 no.6
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    • pp.607-612
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    • 2000
  • Generally, antitumor drugs have strong toxicity and result in damage in normal cells. Previously, lectin has been reported as a tumor cell specific binding protein and tannin as an antitumor substance. In this study, we investigated antitumor activity of lectin-conjugated ellagitannin and used praecoxin A as an ellagitannin source. We injected mouse melanoma cell, B16-F10, on right the femoral region of C57BL/6 mouse. After 10 hours later, first treatment with praecoxin A, lectin-praecoxin A mixiture and lectin-conjugated praecoxin A was carried and followed by injection i.m. every 48 hours. Praecoxin A extended the life of mice up to 14.8% in comparison with the negative control group at 5 mg/kg dose. The life extending ratio of Lectin-praecoxin A mixture was 26.1% at 5 mg/kg dose, and the life extending ratio of lectin-conjugated praecoxin A was 28.7% at 5 mg/kg dose. On the basis of these findings, we suggest that antitumor activities of lectin-praecoxin A mixiture and lectin-conjugated praecoxin A on survival are better than that of praecoxin A.

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Effects of Lectin-conjugated Ellagitannin on the IL-1$\beta$, Gene Expression of Macrophage (Macrophage의 IL-1$\beta$Gene Expression 대한 Lectin-conjugated Ellagitannin의 효과)

  • 김한준;김민수;이민원;최영욱;김하형;이도익
    • YAKHAK HOEJI
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    • v.46 no.3
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    • pp.197-202
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    • 2002
  • Lectin-conjugated praecoxin A, which has developed as a missile antitumor drug, is the one that has conjugated with wheat germ agglutinin (WGA), a kind of carbohydrate-binding protein (lectin) especially bound to melanoma. Praecoxin A is a kind of tannin extracted and purified from plants. Beside this direct antitumor effect as tannins, we have examined an activation of macrophage by lectin-conjugated praecoxin A. We also confirmed the gene expression of IL-1 $\beta$, both in vitro and in vivo. We added 1, 10, 100 $\mu\textrm{g}$/mι of lectin-conjugated praecoxin A, 10 $\mu\textrm{g}$/mι of lectin, 10 $\mu\textrm{g}$/mι of praecoxin A to normal murine macrophage and analyzed the extracted total RNAs by RT-PCR after 4, 8, 12, 24 hours. Our data demonstrated that lectin-conjugated praecoxin A increased IL-1$\beta$, mRNA expression in a dose dependent manner. However, the effectiveness of lectin-conjugated praecoxin A was not superior to lectin and praecoxin A.

Light and Electron Microscopical Observation of the Binding of Lectin to Mouse Intestine (콩과 토란에서 추출한 FITC-Lectin의 마우스 소장조직에 대한 현미경 관찰)

  • 서영주
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.22 no.4
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    • pp.494-499
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    • 1993
  • The morphological and histochemical observation of the lectin binding to intestine in vivo or in vitro was investigated. Our finding demonstrates the validity of semi-quantitative estimates of lectin binding to mouse intestine. The fluorescence patterns obtained after treatment of intestine sections with FITC-conjugated lectin revealed that Kintoki bean lectin (KBL) and Taro tuber lectin (TTL) were localized on the cell membrane, especially the top and upper sites of the villi and showed that KBL was more strongly located than TTL under various conditions. In the reverted intestine of mice fed lectin, the villi were considerably disordered and conspicuously disrupted.

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