• Title, Summary, Keyword: Lectin

Search Result 350, Processing Time 0.032 seconds

Partial Purification of Lectin from Mycoparasitic Species of Trichoderma

  • Singh, Tanuja;Saikia, Ratul;Arora, Dilip K.
    • The Plant Pathology Journal
    • /
    • v.21 no.4
    • /
    • pp.301-309
    • /
    • 2005
  • Trichoderma species/isolates exhibited varied degree of agglutination on sclerotial (Sc) and hyphal (Hy) surface of Macrophomina phaseolina. The agglutination efficiencies on Sc and Hy ranged from $11\;to\;57\%$. Isolates of T. harzianum (Th) and T. viride (Tv) showed greater agglutination on Sc ($23-57\%$) and Hy ($16-47\%$). Different enzymes (trypsin, pepsin, proteinase k, a-chymotrypsin, lyticase and glucosidase) and inhibitors (tunicamycin, cycloheximide, brefeldin A, sodium azide, dithiothreitol and SDS) reduced the agglutination potential of conidia of Th-23/98 and Tv-25/98; however, the extent of response varied greatly in different treatments. Different fractions of Th-23/98 and Tv-25/98 exhibited haemagglutinating reaction with human blood group A, B, AB and O. Haemagglutinating activity was inhibited by different sugars and glycoproteins tested. Crude haemagglutinating protein from outer cell wall protein fraction of Th-23/98 and Tv-25/98 were eluted on Sephadex G-100 column. Initially Th-23/98 and Tv-25/98 exhibited two peaks showing no agglutination activity; however, lectin activity was detected in the third peak. Similar to crude lectin, the purified lectin also exhibited haemagglutinating activity with different erythrocyte source. SDS-PAGE analysis of partially purified lectin revealed single band with an estimated molecular mass of 55 and 52 kDa in Th-23/98 and Tv-25/98, respectively. Trypsin, chymotrypsin and b-1,3-glucanase totally inhibited lectin activity. Similarly, various pH also affected the haemagglutinating activity of Th-23/98 and Tv-25/98. From the present observations, it can be concluded that the recognition/attachment of mycoparasite (T. harzianum and T. viride) to the host surface (M. phaseolina) may be most likely due to lectin-carbohydrate interaction.

Studies on the Preparation of Radioactive iodine Labelled Concanavalin-A, Lectin Extracted from Korean Native Plant “Banha”, and Their Conjugation Products and the Hemagglutination Tests of These Labelled Compounds in Vitro.

  • Kim, You-Sun;Park, Kyung-Bae
    • Nuclear Engineering and Technology
    • /
    • v.10 no.1
    • /
    • pp.1-12
    • /
    • 1978
  • Concanavalin-A, lectin extracted from Korean native plant “Banha”(Pine-llia Termata) and their conjugation products with tyrosine and 5-iodo-6-aminouracil were labelled by radioactive iodiae-125, and these labelled compounds were subjected to a hemagglutination test in vitro. The labelling procedures were presented with respect to labelling yield and the trends on the conjugation reaction of lectin with various amino acids were discussed. The preliminary results on the hemagglutination tests against cancer tissues were presented and the potential clinical applications of these labelled compounds were discussed.

  • PDF

Studies on Lectins From Marine Shells (V) - Isolation and Purification of Letin from Tapes philippinarum. (해양 패류 렉틴성분 연구 (V) - 반지락조개의 렉틴성분 분리정제에 관한 연구)

  • 정시련;김장환;전경희
    • YAKHAK HOEJI
    • /
    • v.31 no.2
    • /
    • pp.52-59
    • /
    • 1987
  • The result of the screening of lectins on 28 species of marine shell fishes(mollusks) showed that 10 species (Tapes philippinarum, Cyclosunetta menstrualis, Neptunea arthritica cumingii, Omphalius pfeifferi carpenteri, Chlorostoma argyrostoma turbinatum, Chiorostoma argyrostoma lischkei, Semisulcosira corea, Neptunea polycosta, Babylonica japonica, Noverita didyma) were present hemagglutinating properties to human A, B, and O group, and animal blood erythrocytes. A new lectin from Tapes philippinarum. was isolated and partially characterized. The lectin was purified by (NH$_4$)$_2$SO$_4$ precipitation and ion exchange chromatography on DE 53 column. Six fractions were obtained from DE 53 column by salt gradient elution but only 0.3M, and 0.4M NaCl fraction had strong lectin activity. On its 0.3M NaCl fraction, purity was identified by polyacrylamide gel electrophoresis. This lectin was inhibited by N-acetyl-D-galactosamine. It seems that two kinds of lectin react as antigen by immunochemical studies.

  • PDF

Purification and Characterization of A New Lectin from Marine Animal Lunella coronata coreensis (해양동물 눈알고둥으로부터 새로운 렉틴 성분의 분리 및 정제)

  • So, Myung-Suk;Suh, Young-Ah;Jeune, Kyung-Hee;Chung, See-Ryun
    • 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.

  • PDF

Mitotic Stimulation and Cancer Cell Agglutination of the Lectin from Lentinus edodes (표고버섯 렉틴의 림프구 자극 분열 및 암 세포 응집 효과)

  • 문익재;정시련;전경희
    • 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.

  • PDF

Immuno Activation of Lectin-Conjugated Praecoxin A on IL-6, IL-12 Expression

  • Joo, Seong-Soo;Chang, Jae-Kwon;Park, Jeong-Hwan;Kang, Hee-Chul;Lee, Do-Ik
    • Archives of Pharmacal Research
    • /
    • v.25 no.6
    • /
    • pp.954-963
    • /
    • 2002
  • Lectin-conjugated praecoxin A is a compound, which is combined Wheat Germ Agglutinin (WGA) Lectin with praecoxin A and also known to have an anti-tumor activity. In our lab, in order to investigate its immune reaction other than the anti-tumor activity ever known, we examined cytokines such as IL-6 and IL-12 through their mRNA expressions, which are generally secreted by macrophage both in vivo and in vitro. To analyze, we used RT-PCR for total RNAs of macrophages. As a result, we obtained that both in vitro and in vivo, lectin-conjugated praecoxin A showed an interesting increase on IL-6 and IL-12 even though it may be little hard to say the conjugated form is absolutely more effective than that of lectin or praecoxin A alone for immune response activities. Those results suggest that the conjugated form may give an additional opportunity in a future therapeutic use over its immuno activation properties.

Purification and Characterization of Hemagglutinating Protein from Rhizome of Alisma orientale (택사(Alismatis Rhizoma) Hemagglutinating Protein의 정제와 특성)

  • 박종옥;김경순;선우근옥
    • Journal of the Korean Society of Food Science and Nutrition
    • /
    • v.24 no.4
    • /
    • pp.587-593
    • /
    • 1995
  • Lectin was purified by using $(NH_4)_2SO_4$, DEAE-cellulose ion-exchange chromatography and Sephadex G-150 column chromatography from Alismatis Rhizoma(AR). The specific activity of AR lectin was 50, 441units/mg, and purification folds were 114. The AR lectin agglutinated human erythrocytes of all types(A, B, O, AB). The molecular weight of AR lectin was estimated about 90, 500 daltons by gel filtration and each subunits were 42,000, 27,000 and 22,500 daltons on SDS-PAGE respectively. The hemagglutinating activity of the lectin was inhibited by sialic acid, glucose, ribose, galactose, sucrose, and lactose. It was also inhibited by cations such as $Hg^{++},\;Fe^{++},\;Cu^{++}\;and\;Pb^{++}$.

  • PDF

Preparation of Alginate/Chitosan Microcapsules and Enteric Coated Granules of Mistletoe Lectin

  • Lyu, Su-Yun;Kwon, Young-Ju;Joo, Hye-Jin;Park, Won-Bong
    • Archives of Pharmacal Research
    • /
    • v.27 no.1
    • /
    • pp.118-126
    • /
    • 2004
  • The aqueous extract of European mistletoe (Viscum album, L.) has been used in cancer therapy. The purified mistletoe lectins, main components of mistletoe, have demonstrated cytotoxic and immune-system-stimulating activities. Korean mistletoe (Viscum album L. coloratum), a subspecies of European mistletoe, has also been reported to possess anticancer and immunological activities. A galactose- and N-acetyl-D-galactosamine-specific lectin (Viscum album L. coloratum agglutinin, VCA) with Mr 60 kDa was isolated from Korean mistletoe. Mistletoe preparations have been given subcutaneously due to the low stability of lectin in the gastrointestinal (GI) tract. In the present study, we investigated the possibility of alginate/chitosan microcapsules as a tool for oral delivery of mistletoe lectin. In addition, our strategy has been to develop a system composed of stabilizing cores (granules), which contain mistletoe lectin, extract or powder, coated by a biodegradable polymer wall. Our results indicated that successful incorporation of VCA into alginate/chitosan microcapsules has been achieved and that the alginate/chitosan microcapsule protected the VCA from degradation at acidic pH values. And coating the VCA with polyacrylic polymers, Eudragit, produced outstanding results with ideal release profiles and only minimal losses of cytotoxicity after manufacturing step. The granules prepared with extract or whole plant produced the best results due to the stability in the extract or whole plant during manufacturing process.

Production and Isolation of IgY Antibody Raised Against a Lectin Obtained from Maackia fauriei (Maackia fauriei 유래 렉틴에 대한 IgY 항체의 생성 및 분리)

  • Chung Young Yun;Jung Eui Cha;Lee Hyun Jung;Kim HaHyung
    • YAKHAK HOEJI
    • /
    • v.49 no.1
    • /
    • pp.6-10
    • /
    • 2005
  • Immunoglobulin Y (IgY) obtained from chicken as the immunization host brings several advantages to antibody production, such as improved yield, lower cost, longer stability and higher specificity than mammalian immunoglobulin. In the present study, we attempted to produce IgY against a sialic acid-binding lectin, Maackia fauriei agglutinin (MFA), from egg yolk of white Leghorn hens. For the isolation of IgY from egg yolk, we applied a water dilution method. The weekly yield of IgY was determined by enzyme-linked immunosorbent assay, with a final yield of anti-MFA IgY from total IgY of approximately $1\%$. The yielded IgY were used to prepare IgY-affinity column conjugated with CNBr-activated Sepharose 4B, which resulted in the lectin being successfully purified in a single step from Maackia fauriei. This purified lectin exhibited the same hemagglutination activity as lectin purified using conventional purification methods.

The Effect of Acute Sinusitis on the Ultrastructure and Sialic Acid Distribution on the Sinus Mucosa Cell Surface of the Rabbit (실험토끼 상악동염이 상피세포 표면의 미세구조변화와 Sialic acid의 분포에 미치는 영향)

  • Kim, Soo-Jin;Lee, Eun-Jung
    • Applied Microscopy
    • /
    • v.32 no.2
    • /
    • pp.163-170
    • /
    • 2002
  • Experimatal maxillary sinusitis was induced in New Zealand white rabbits by blocking the maxillary sinus ostium. The distribution of lectin receptors was explored in the mucosa with induced maxillary sinusitis using colloidal gold label complex with lectin WGA purified from wheat germ (Triticum vulgaris). The lectin WGA gold complex, shown to recognize GlcNac (N-acetylglucosamine) and NeuNAc (N-acetylneuraminic acid) regions, was applied to detect binding sites in Lowicryl HM 20 sections and viewed under the electron microscope. An increased height of the cylindric cells, ciliary loss and hyperplasia of the secretory cells were observed. Examination of normal sinus mucosa labeled with gold-labeled lectins showed the distribution of sialoglycoconjugates to be mainly in the ciliary layer and the granules in the secretory cells. Inflamed mucosa had increased labeling intensity of gold-labeled WGA in the cilia and the secretory granules. These results indicate that lectin WGA receptors are located in the cilia and secretory granules. Specific changes in the lectin binding pattern were apparent in the inflamed mucosa in the experimentally induced acute sinusitis, in comparison with normal mucosa, conceivably as a part of host defense reactions.