Relevant bibliographies by topics / Lectin

Academic literature on the topic 'Lectin'

Author: Grafiati
Published: 4 June 2021
Last updated: 22 December 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Contents

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Lectin.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Lectin"

1

Flower, Robert L. P. "Innate Immunity in Lobsters: Partial Purification and Characterization of a Panulirus cygnus Anti-A Lectin." ISRN Hematology 2012 (March 5, 2012): 1–5. http://dx.doi.org/10.5402/2012/964986.

Full text
Abstract:
A lectin detected in haemolymph from the Australian spiny lobster Panulirus cygnus agglutinated human ABO Group A cells to a higher titre than Group O or B. The lectin also agglutinated rat and sheep erythrocytes, with reactivity with rat erythrocytes strongly enhanced by treatment with the proteolytic enzyme papain, an observation consistent with reactivity via a glycolipid. The lectin, purified by affinity chromatography on fixed rat-erythrocyte stroma, was inhibited equally by N-acetylglucosamine and N-acetylgalactosamine. Comparison of data from gel filtration of haemolymph (behaving as a 1,800,000 Da macromolecule), and polyacrylamide gel electrophoresis of purified lectin (a single 67,000 Da band), suggested that in haemolymph the lecin was a multimer. The purified anti-A lectin autoprecipitated unless the storage solution contained chaotropic inhibitors (125 mmol/L sucrose: 500 mmol/L urea). The properties of this anti-A lectin and other similar lectins are consistent with a role in innate immunity in these invertebrates.
APA, Harvard, Vancouver, ISO, and other styles
2

Kothari, Sajani, Rebecca Heineman, and Rene Harrison. "Optimizing Lectin Staining Methodology to Assess Glycocalyx Composition of Legionella-Infected Cells." Undergraduate Research in Natural and Clinical Science and Technology (URNCST) Journal 7, no. 7 (July 17, 2023): 1–10. http://dx.doi.org/10.26685/urncst.490.

Full text
Abstract:
Introduction: Legionella is a gram-negative bacterium that replicates intracellularly within macrophages. Legionella utilizes effector proteins to hijack ER-Golgi vesicle trafficking to sustain proliferation in its intracellular niche. Legionella has a considerable influence on O-glycosylation but not N-glycosylation events in the Golgi of infected cells. This research aims to optimize the use of fluorescent lectins, which are proteins that bind carbohydrates, to effectively label host-cell glycocalyx during Legionella infection. Methods: Epifluorescence imaging or flow cytometry were used to optimize the lectin staining methodology. We noted that the most effective conditions for lectin-labeling were when live HeLa cells were incubated with lectins diluted in Hank’s balanced salt solution (HBSS) with 3% Bovine serum albumin (BSA) for 10-30 minutes at 4 °C. Results: Incubating suspended cells with lectins necessitated smaller lectin concentrations, whereas lectin labeling of adherent cells required considerably larger concentrations. Wheat germ agglutinin (WGA) lectin mean fluorescence intensity (MFI) was concentration-dependent, but Concanavalin A (ConA) and Maclura pomifera (MPA) MFIs did not alter substantially with increasing lectin concentrations. Discussion: The optimal lectin concentration required was lectin-specific and based on whether the lectin fluorescence was assessed using flow cytometry or epifluorescence. Furthermore, the use of phosphate-buffered saline (PBS) for lectin dilution, cell permeabilization for intracellular labelling, and incubation of lectins in fixed cells reduced productive labelling of lectins on cell surfaces because it inhibited the lectin's ability to effectively bind the associated carbohydrate structure. Conclusion: Further research using diverse lectins on U937 macrophages is necessary to reach a definitive conclusion on the effect of Legionella on the overall host-cell glycocalyx composition during infection of these relevant immune cells.
APA, Harvard, Vancouver, ISO, and other styles
3

Ogilvie, Mary L., JoAnn Wilson Byl, and T. Kent Gartner. "Platelet Aggregation Is Stimulated by Lactose-lnhibitable Snake Venom Lectins." Thrombosis and Haemostasis 62, no. 02 (1989): 704–7. http://dx.doi.org/10.1055/s-0038-1646887.

Full text
Abstract:
SummaryFive lactose-specific lectins from snake venoms were tested for the ability to stimulate the aggregation of human platelets. Three of the lectins, bushmaster (Lachesis muta), cottonmouth (Aricistrodon piscivorous leukostoma) and rattlesnake (Crotalus atrox) lectins, consistently stimulated secretion and aggregation. Thrombolectin (Bothrops atrox) occasionally caused aggregation. Copperhead (Agkistrodon contortrix contortrix) lectin did not by itself cause platelet aggregation. Lactose, a specific inhibitor of hemagglutination mediated by these lectins was a potent inhibitor of lectin-induced aggregation. Antiserum specific for bushmaster lectin inhibited aggregation by bushmaster lectin. In contrast, the same antiserum and anti-cottonmouth lectin serum enhanced aggregation by low levels of the other lectins.A variety of substances were assayed in the aggregometer for the ability to inhibit aggregation in response to these lectins. Both secretion and aggregation were inhibited by PGI2 and PGEx. Furthermore, lectin-induced aggregation was completely blocked by trifluoperazine and partially blocked by indomethacin. Monoclonal antibodies specific for GP IIb/IIIa (AP2, A2A9, LJP5, LJCP8) but not monoclonals directed against other platelet membrane proteins (API and AP3) inhibited lectin-induced aggregation. The peptide Arg-Gly-Asp-Ser but not Arg-Ala-Asp-Ser was a potent inhibitor of aggregation.
APA, Harvard, Vancouver, ISO, and other styles
4

Barre, Annick, Mathias Simplicien, Hervé Benoist, Els J. M. Van Damme, and Pierre Rougé. "Mannose-Specific Lectins from Marine Algae: Diverse Structural Scaffolds Associated to Common Virucidal and Anti-Cancer Properties." Marine Drugs 17, no. 8 (July 26, 2019): 440. http://dx.doi.org/10.3390/md17080440.

Full text
Abstract:
To date, a number of mannose-specific lectins have been isolated and characterized from seaweeds, especially from red algae. In fact, man-specific seaweed lectins consist of different structural scaffolds harboring a single or a few carbohydrate-binding sites which specifically recognize mannose-containing glycans. Depending on the structural scaffold, man-specific seaweed lectins belong to five distinct structurally-related lectin families, namely (1) the griffithsin lectin family (β-prism I scaffold); (2) the Oscillatoria agardhii agglutinin homolog (OAAH) lectin family (β-barrel scaffold); (3) the legume lectin-like lectin family (β-sandwich scaffold); (4) the Galanthus nivalis agglutinin (GNA)-like lectin family (β-prism II scaffold); and, (5) the MFP2-like lectin family (MFP2-like scaffold). Another algal lectin from Ulva pertusa, has been inferred to the methanol dehydrogenase related lectin family, because it displays a rather different GlcNAc-specificity. In spite of these structural discrepancies, all members from the five lectin families share a common ability to specifically recognize man-containing glycans and, especially, high-mannose type glycans. Because of their mannose-binding specificity, these lectins have been used as valuable tools for deciphering and characterizing the complex mannose-containing glycans from the glycocalyx covering both normal and transformed cells, and as diagnostic tools and therapeutic drugs that specifically recognize the altered high-mannose N-glycans occurring at the surface of various cancer cells. In addition to these anti-cancer properties, man-specific seaweed lectins have been widely used as potent human immunodeficiency virus (HIV-1)-inactivating proteins, due to their capacity to specifically interact with the envelope glycoprotein gp120 and prevent the virion infectivity of HIV-1 towards the host CD4+ T-lymphocyte cells in vitro.
APA, Harvard, Vancouver, ISO, and other styles
5

Bonnardel, François, Julien Mariethoz, Serge Pérez, Anne Imberty, and Frédérique Lisacek. "LectomeXplore, an update of UniLectin for the discovery of carbohydrate-binding proteins based on a new lectin classification." Nucleic Acids Research 49, no. D1 (November 11, 2020): D1548—D1554. http://dx.doi.org/10.1093/nar/gkaa1019.

Full text
Abstract:
Abstract Lectins are non-covalent glycan-binding proteins mediating cellular interactions but their annotation in newly sequenced organisms is lacking. The limited size of functional domains and the low level of sequence similarity challenge usual bioinformatics tools. The identification of lectin domains in proteomes requires the manual curation of sequence alignments based on structural folds. A new lectin classification is proposed. It is built on three levels: (i) 35 lectin domain folds, (ii) 109 classes of lectins sharing at least 20% sequence similarity and (iii) 350 families of lectins sharing at least 70% sequence similarity. This information is compiled in the UniLectin platform that includes the previously described UniLectin3D database of curated lectin 3D structures. Since its first release, UniLectin3D has been updated with 485 additional 3D structures. The database is now complemented by two additional modules: PropLec containing predicted β-propeller lectins and LectomeXplore including predicted lectins from sequences of the NBCI-nr and UniProt for every curated lectin class. UniLectin is accessible at https://www.unilectin.eu/
APA, Harvard, Vancouver, ISO, and other styles
6

Melgarejo, Luz Marina, Nohora Vega, and Gerardo Pérez. "Isolation and characterization of novel lectins from Canavalia ensiformis DC and Dioclea grandiflora Mart. ex Benth. seeds." Brazilian Journal of Plant Physiology 17, no. 3 (September 2005): 315–24. http://dx.doi.org/10.1590/s1677-04202005000300006.

Full text
Abstract:
Two lectins were isolated from Canavalia ensiformis and Dioclea grandiflora seeds. Gel filtration produced a fraction corresponding to Con A or D. grandiflora lectin while erythroagglutination assays revealed a distinct fraction presenting a lectin that agglutinates human red blood cells (RBCs) but not rabbit RBCs. Hydrophobic interaction chromatography showed that the latter fraction yielded a protein that readily agglutinates human erythrocytes; the lectin was also purified by affinity chromatography on Lac-Sepharose showing similar properties to that of the Phenyl-Sepharose-purified lectin. Despite minor differences (carbohydrate content or A1%1cm), the two lectins showed similar molecular properties in that they consisted of two non-covalently linked monomers having a Mr of 29-30 kDa and their pI values indicated that both lectins were slightly acidic proteins. The C. ensiformis lectin (CEL-II) and D. grandiflora lectin (DGL-II) specifically recognised the H-type 2 blood group (alpha-L-Fuc (1-2)-beta-D-Gal (1-4)-beta-D-GlcNAc-O-R), while binding to H-type 1, H-type 3, H-type 4, Leª or Le y was weaker. Carbohydrate inhibition of erythroagglutination showed that simple sugars were weakly recognised by the lectins, if at all. The N-terminal region presented a unique sequence hitherto found only in some Diocleinae lectins (designated type II). The overall results confirmed the existence of a second distinct lectin type, phylogenetically close to Diocleinae species. The data indicate a functional similarity among lectins of this type which possesses distinctive characteristics differentiating them from "classical" Man/Glc lectins.
APA, Harvard, Vancouver, ISO, and other styles
7

Petrova, Natalia, and Natalia Mokshina. "Using FIBexDB for In-Depth Analysis of Flax Lectin Gene Expression in Response to Fusarium oxysporum Infection." Plants 11, no. 2 (January 7, 2022): 163. http://dx.doi.org/10.3390/plants11020163.

Full text
Abstract:
Plant proteins with lectin domains play an essential role in plant immunity modulation, but among a plurality of lectins recruited by plants, only a few members have been functionally characterized. For the analysis of flax lectin gene expression, we used FIBexDB, which includes an efficient algorithm for flax gene expression analysis combining gene clustering and coexpression network analysis. We analyzed the lectin gene expression in various flax tissues, including root tips infected with Fusarium oxysporum. Two pools of lectin genes were revealed: downregulated and upregulated during the infection. Lectins with suppressed gene expression are associated with protein biosynthesis (Calreticulin family), cell wall biosynthesis (galactose-binding lectin family) and cytoskeleton functioning (Malectin family). Among the upregulated lectin genes were those encoding lectins from the Hevein, Nictaba, and GNA families. The main participants from each group are discussed. A list of lectin genes, the expression of which can determine the resistance of flax, is proposed, for example, the genes encoding amaranthins. We demonstrate that FIBexDB is an efficient tool both for the visualization of data, and for searching for the general patterns of lectin genes that may play an essential role in normal plant development and defense.
APA, Harvard, Vancouver, ISO, and other styles
8

Taatjes, D. J., L. A. Barcomb, K. O. Leslie, and R. B. Low. "Lectin binding patterns to terminal sugars of rat lung alveolar epithelial cells." Journal of Histochemistry & Cytochemistry 38, no. 2 (February 1990): 233–44. http://dx.doi.org/10.1177/38.2.1688898.

Full text
Abstract:
We used post-embedding cytochemical techniques to investigate the lectin binding profiles of rat lung alveolar epithelial cells. Sections from rat lung embedded in the hydrophilic resin Lowicryl K4M were incubated either directly with a lectin-gold complex or with an unlabeled lectin followed by a specific glycoprotein-gold complex. The binding patterns of the five lectins used could be divided into three categories according to their reactivity with alveolar epithelial cells: (a) the Limax flavus lectin and Ricinus communis I lectin bound to both type I and type II cell plasma membranes; (b) the Helix pomatia lectin and Sambucus nigra L. lectin bound to type II but not type I cells; and (c) the Erythrina cristagalli lectin reacted with type I cells but was unreactive with type II cells. The specificity of staining was assessed by control experiments, including pre-absorption of the lectins with various oligosaccharides and enzymatic pre-treatment of sections with highly purified glycosidases to remove specific sugar residues. The results demonstrate that these lectins can be used to distinguish between type I and type II cells and would therefore be useful probes for investigating cell dynamics during lung development and remodeling.
APA, Harvard, Vancouver, ISO, and other styles
9

Levine, E., R. Werner, and G. Dahl. "Cell-cell channel formation and lectins." American Journal of Physiology-Cell Physiology 261, no. 6 (December 1, 1991): C1025—C1032. http://dx.doi.org/10.1152/ajpcell.1991.261.6.c1025.

Full text
Abstract:
The oocyte cell-cell channel assay was used to investigate determinants of the rate of channel formation. After injection of connexin-specific mRNA, oocytes accumulate a pool of precursors from which cell-cell channels can form after oocytes are paired. Channel formation was found to be increased if oocytes are pretreated with lectins before pairing. Several lectins differing in their carbohydrate binding affinities can exert this effect. Lectin-specific sugars suppress the effect on cell-cell channel formation only if the sugar is mixed with the lectin before application to the oocyte. If the lectin is first bound to the oocyte and then the sugar is added, no significant inhibition is seen. The promotion of channel formation by lectins is enhanced by adding an incubation period in regular medium after lectin treatment, before pairing of the oocytes. Electron microscopic studies with gold-conjugated lectins show that the lectin receptors are clustered on the free membrane surface and are taken up in endocytotic vesicles. These data suggest that the observed acceleration of cell-cell channel formation by lectins can be attributed to the removal of steric hindrance, which is a consequence of clustering of the bulky glycoprotein lectin receptors as well as of the removal from the surface by endocytosis.
APA, Harvard, Vancouver, ISO, and other styles
10

Gerhardus, M. J. T., J. M. C. Baggen, W. P. W. Van Der Knaap, and T. Sminia. "Analysis of surface carbohydrates of Trichobilharzia ocellata miracidia and sporocysts using lectin binding techniques." Parasitology 103, no. 1 (August 1991): 51–59. http://dx.doi.org/10.1017/s003118200005928x.

Full text
Abstract:
Miracidia and in vitro-derived primary sporocysts of the avian schistosome Trichobilharzia ocellata were studied for the expression and the characteristics of glycoconjugate moieties comprising the surface coat. Using a panel of 9 peroxidase labelled lectins, several different lectin binding sites were demonstrated on the larvae. Fixed miracidia have binding sites for 7 of the lectins; wheat-germ agglutinin binds to both the ciliated plates and the tegumental ridges between them; the other 6 lectins bind to the plates only. Three of the miracidia-binding lectins, wheat-germ agglutinin, concanavalin A and peanut agglutinin, also bind to fixed sporocysts. Since the miracidial ridges are devoid of binding sites for concanavalin A and peanut agglutinin, whereas the sporocyst tegument binds these lectins, it appears that these sites become exposed during or shortly after transformation. In saturation experiments, low concentrations of peanut agglutinin and concanavalin A are bound more avidly by sporocysts than by miracidia, indicating a higher binding affinity of the former. The two larval forms do not differ in affinity for wheat-germ agglutinin but they have different binding capacities; when offered in high concentrations, more of this lectin is bound by sporocysts than by miracidia. Lectin binding was competitively inhibited by adding the appropriate free saccharides. Live larvae showed the same lectin binding pattern as did fixed specimens. Proteinase treatment reduced lectin binding to living and, to a lesser extent, to fixed larvae, suggesting that binding sites are constituents of proteoglycoconjugates. After SDS–PAGE of extracts from miracidia and sporocysts and subsequent Western blotting, some of the lectins failed to bind glycoproteins, others reacted with an array of bands. The patterns differed among the lectins and each lectin gave different patterns for miracidia and sporocysts. The results obtained with these two lectin-binding techniques support the conclusion that stage-specific proteoglycoconjugates occur at the surface of T. ocellata larvae.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "Lectin"

1

Lucca, Rosemeire Aparecida da Silva de. "Propriedades físico-químicas da lectina KM+ monitoradas por dicroismo circular (CD) e fluorescência. Estimativa do conteúdo de estrutura secundaria por CD." Universidade de São Paulo, 1994. http://www.teses.usp.br/teses/disponiveis/76/76132/tde-02042014-100315/.

Full text
Abstract:
Uma nova lectina extraída da semente de Artocarpus integrifólia, denominada KM+ foi recentemente descrita. KM+ e haptotática para neutrófilos, promove a aglutinação de hemácias dos grupos A, B, 0, estimula a proliferação de linfócitos do baço de camundongos e liga-se em α D-manose, α metil manosidio e α D-glicose. Esta lectina é composta por quatro monômeros, com peso molecular de 13.150 daltons cada, unidos por interações não covalentes. KM+ contem 1,8% de carboidratos e apresentou quatro isoformas com pontos isoelétricos entre 4,2 e 5,2. Este trabalho teve como objetivos estudar modificações estruturais de KM+ em função de parâmetros como temperatura, força iônica, pH, agentes desnaturantes, ligação com D-manose, monitoradas por dicroísmo circular (CD) e fluorescência. CD também foi utilizado para estimar o conteúdo de estrutura secundaria de KM+, utilizando-se dois programas descritos na literatura: SSE (Secondary Structure Estimation), que utiliza o método dos mínimos quadrados para a estimativa da estrutura secundaria e obtenção dos espectros básicos, baseados nos dados cristalográficos de proteínas de .estrutura resolvida; CCA (Convex Constraint Analisys) que utiliza o algoritmo simplex e a partir dos espectros de CD das proteínas de referencia calcula os espectros das componentes básicas. Para a estimativa das frações de estrutura secundária o segundo método utiliza o programa Lincomb. Os espectros de CD foram registrados no intervalo de 185 a 260 nm. O conteúdo em estrutura secundária, estimado pelo programa SSE foi: 0% de α-hélice, 41% de folha β, 27% de volta β e 32,3 de estrutura desordenada; pelo programa CCA foi: 1% de α-hélice, 35% de folha β anti-paralela, 21% de volta β e/ou folha β paralela, 15% de contribuições de aromáticos e/ou ligações dissulfeto, 28% de estrutura desordenada. Os desvios médios quadráticos para os programas SSE e CCA foram 12% e 1%, respectivamente. Portanto a lectina KM+ é principalmente constituída por estruturas tipo folha β e tipo desordenada. A curva calculada pelo programa CCA foi mais bem estimada, pois tem o desvio médio quadrático 12 vezes menor que o do programa SSE. Este resultado, provavelmente ocorre devido aos seguintes fatores: (i) no programa CCA, o espectro da proteína a ser analisada e alinhado com os espectros das proteínas de referência, influenciando no calculo dos espectros básicos; (ii) maior número de proteínas com estrutura β no grupo de referência do programa CCA. A estabilidade de KM+ em função da temperatura tem comportamento diferente em tampão sódio fosfato (PBS) daquele observado em água. Em PBS, quando a amostra esta a 70°C, a forma do espectro de CD mostrou-se consistente com um espectro de proteína desnaturada. Comumente, um espectro de proteína desnaturada caracteriza-se pela perda da estrutura secundaria predominante e aumento da estrutura desordenada. Em água, também a 70°C, na região da estrutura β (216 nm) surge uma nova banda e na região da estrutura desordenada (195 nm) aparece uma banda com valores positivos mimetizando um espectro da estrutura α-hélice. Esta diferença de comportamento pode ser devida à força iônica. A desorganização promovida na molécula de KM+ por cloreto de guanidina foi típica de desnaturação. o máximo da emissão de fluorescência, da KM+ em PBS pH 7,2, foi a 328 nm, característico de resíduos de triptofano protegidos do solvente. Este máximo mudou para 340 nm em pH 10,5. Este resultado indica mudanças no ambiente químico do triptofano neste pH. O deslocamento para a região do vermelho indica, que em pH. os resíduos de triptofano estio em maior contato com o solvente. O número de sitios ligantes de D-manose J)a molécula de KM+, foi estimado pela supressão da fluorescência promovida pelo D-manose. Esta estimativa foi baseada na suposição de que todos os sítios ligantes de D-manose estivessem próximos aos resíduos de triptofano. A relação encontrada foi de 2 moles de D-manose/mol de KM+
Recently a new lectin, KM+, isolated from Artocarpus integrifolia seeds was described. KM+ induces neutrophil migration, agglutination of human red blood cells, proliferation of mouse spleen cells and binding with monosacharides D-mannose, D-glicose and α-metil mannoside. This glycoprotein is composed of four monomers, assembled by non covalent bonds, has 500 aminoacids residues/mol, with a Molecular Weight of 52,000 Daltons and 1.8% of carbohydrates [27]. In this work structural changes of KM+ was studied as a function of temperature, pH, chemical denaturing agents as well as the binding with D-mannose. These changes were monitored by circular dichroism (CD) and fluorimetry. Circular Dichroism (CD) spectroscopy was used for the analysis of the secondary structure of KM+ in solution due do its capacity to indicate the presence and to estimate the proportion of α-helix, β-sheet, β-turn and unordered conformations. This measurent can be regarded as a function of the relative orientation of the chromophores responsible for their chiroptical activity. CD spectroscopy is also one of the methods of choice for monitorization of conformational changes in proteins as a function of solvents, pH, temperature, ionic strength and specific or non specific binding. Two programs which are in use for estimation of secondary structure: SSE, using the linear least squares method and CCA, using the simplex method, were evaluated in the present work. SSE uses a set of proteins with known X-ray data as the basis for evaluation while CCA uses only pure proteins experimental CD spectra. Fluorescence spectroscopy is very useful to monitore of protein conformational changes in solution due to the presence of intrinsic fluorophores. Fluorescence Measurements were performed at 25°C. Samples were excited at 280 nm and the emission was monitored in the range 290-450 nm. The maximum emission as a function of pH was at pH 7.0. The wavelength for maximum emission changed from 328 nm at pH 7.0 to 340 nm at pH 10.5. CD spectra were recorded over the range of 185 up to 260 nm. The Secondary structure content estimated by SSE program was: 0% α-helix, 41% β-sheet, 26% β-turn and 32% random with RMS of 12% and CCA program was: 1% α-helix, 35% antiparallel β-sheet, 21% β-turn and/or parallel B-sheet, 28% random, 15% aromatics contributions and dissulfide linkages with RMS of 1%. The fractions of secondary structure obtained when using CCA program were more consistent than those of SSE program. The simulation by CCA program was better probably due to its desconvolution of the spectral contribution of the common secondary structures using experimental CD curves of proteins. The stability of KM+, in PBS, as a function of temperature changes above 55°C but only at 70°C the shape of the CD spectrum is consistent with the loss of the native ordered secondary structure that should accompany protein unfolding. CD spectra of KM+ in water showed conformational changes as a function of temperature was not consistent with denaturated proteins. The unfolding of KM+ by GdnCl and SDS resulted in CD spectroscopic changes: consistent with the increased random structure and disappearance of beta sheet. Using the two denaturing agents together GdnCl and temperature, the denaturation was observed at lower decreased both GdnCl concentration and at lower temperature. The estimation of the number of binding sites for D-mannose was obtained through the fluorescence intensity decrease due to a quenching effect of D-mannose and showed that the stoichiometry of binding was 2 moles of D-mannoseimol of lectin
APA, Harvard, Vancouver, ISO, and other styles
2

Correia, Jorge Luis Almeida. "PurificaÃÃo, caracterizaÃÃo parcial e potencialidade biotecnolÃgica de trÃs lectinas de sementes de espÃcies de Leguminosae da subtribo Diocleinae." Universidade Federal do CearÃ, 2015. http://www.teses.ufc.br/tde_busca/arquivo.php?codArquivo=17238.

Full text
Abstract:
CoordenaÃÃo de AperfeiÃoamento de Pessoal de NÃvel Superior
FundaÃÃo Cearense de Apoio ao Desenvolvimento Cientifico e TecnolÃgico
Conselho Nacional de Desenvolvimento CientÃfico e TecnolÃgico
Leguminosae is recognized by the large amount of isolated and characterized lectins, especially seeds. In this group stand out proteins extracted from species belonging to subtribe Diocleinae, the number of studies in different areas of knowledge. Lectins can be defined as proteins or glycoproteins which are not originated from a body's immune response and have the ability to recognize and bind reversibly to mono or oligosaccharides particular without, however, altering their chemical structures. Different works in our group are structurally haracterizing these proteins as well as elucidating some possible biotechnological applications for these molecules. In this sense, the objective of this study was to isolate and characterize lectins of different species of Leguminosae of Diocleinae subtribe and test them for toxicity to Artemia sp. naupilos, The effect on the smooth muscle of blood vessels and the detention lectin matrix agarose previously activated with cyanogenic bromide (CNBr). Were isolated and characterized the lectin Dioclea sclerocarpa, Dioclea lasiocarpa and Dioclea lasiophylla. Were also made circular dichroism studies on lectin Dioclea sclerocarpa and Dioclea lasiocarpa. The lectin Dioclea lasiophylla was tested against Artemia sp. order to assess their toxicity and was also immobilized on agarose matrix. We evaluated the effect of lectin Dioclea lasiocarpa in the smooth muscle of blood vessels. The knowledge gained from the three scientific articles published in this thesis is a major breakthrough in this promising field of study that has been continuously growing for biotechnological applications.
A famÃlia Leguminosae à reconhecida pela grande quantidade de lectinas isoladas e caracterizadas, especialmente de sementes. Neste grupo se destacam as proteÃnas extraÃdas de espÃcies pertencentes a subtribo Diocleinae, pela quantidade de estudos em diferentes Ãreas do conhecimento. Lectinas podem ser definidas como proteÃnas ou glicoproteÃnas que nÃo sÃo originadas a partir de uma resposta imunolÃgica do organismo e possuem a capacidade de reconhecer e se ligar reversivelmente a mono ou oligossacarÃdeos especÃficos sem, no entanto, alterar suas estruturas quÃmicas. Diferentes trabalhos no nosso grupo vÃm caracterizando estruturalmente essas proteÃnas, bem como elucidando algumas possÃveis aplicaÃÃes biotecnolÃgicas para essas molÃculas. Neste sentido, o objetivo deste trabalho foi isolar e caracterizar lectinas de diferentes espÃcies de Leguminosae da subtribo Diocleinae e testa-las com relaÃÃo à toxicidade para naupilos de Artemia sp., o efeito na musculatura lisa de vasos sanguÃneos e a imobilizaÃÃo de lectina em matriz de agarose previamente ativada com brometo cianogÃnico (CNBr). Foram isoladas e caracterizadas as lectinas de Dioclea sclerocarpa, Dioclea lasiocarpa e Dioclea lasiophylla. TambÃm foram feitos estudos de dicroÃsmo circular na lectina de Dioclea sclerocarpa e Dioclea lasiocarpa. A lectina de Dioclea lasiophylla foi testada contra Artemia sp.de forma a avaliar sua toxicidade e tambÃm foi imobilizada em matriz de agarose. Foi avaliado o efeito da lectina de Dioclea lasiocarpa na musculatura lisa de vasos sanguineos. O conhecimento acumulado a partir dos trÃs artigos cientÃficos publicados nesta tese constitui um grande avanÃo no neste campo promissor de estudo que vem em contÃnuo crescimento para aplicaÃÃo biotecnolÃgica.
APA, Harvard, Vancouver, ISO, and other styles
3

Dalvina, Correia da Silva Michele. "Aplicações biotecnológicas das lectinas ClaveLL (Cladonia verticillaris Lichen Lectin) E BmoLL (Bauhinia monandra Leaf Lectin)." Universidade Federal de Pernambuco, 2008. https://repositorio.ufpe.br/handle/123456789/1424.

Full text
Abstract:
Made available in DSpace on 2014-06-12T15:50:03Z (GMT). No. of bitstreams: 2 arquivo1537_1.pdf: 9274527 bytes, checksum: 3a63d7fc1e96554e66a516ab6af4bddd (MD5) license.txt: 1748 bytes, checksum: 8a4605be74aa9ea9d79846c1fba20a33 (MD5) Previous issue date: 2008
Lectinas são proteínas presentes em diferentes organismos, dos quais são isoladas; possuem origem não imune e habilidade para se ligarem a carboidratos ou glicoconjugados, através de sítios específicos; forças de interação eletrostática e a presença de íons metálicos podem influenciar o processo de ligação. Neste trabalho, foram avaliadas a lectina de folhas de Bauhinia monandra, BmoLL, e a lectina do líquen Cladonia verticillaris, ClaveLL. A investigação e conseqüente emprego biotecnológico de lectinas como proteínas com ação antimicrobiana e inseticida, bem como sua utilidade em histoquímica no estudo e diagnóstico de patologias, estimularam a realização desta Tese. As lectinas foram avaliadas quanto a potencial ação contra bactérias e espécies fúngicas do gênero Fusarium, como proteínas inseticidas para a espécie de cupins Nasutitermes corniger, e também como ferramentas histoquímicas para a investigação histopatológica dos hipocampos de pacientes com doença de Alzheimer. BmoLL e ClaveLL são ativas contra diferentes espécies de Fusarium (F. solani, F. lateritium, F. fusarioides, F. moniliforme e F. verticiloides com BmoLL; e Fusarium verticiloides, F. descemcellulare, F. fusarioides, F. oxysporum e F. moniliforme com ClaveLL) e são hábeis em aglutinar, como também inibir a proliferação de bactérias Gram-positivas e Gram-negativas. BmoLL e ClaveLL possuem ação não repelente e inseticida contra N. corniger. Em histoquímica de hipocampo, BmoLL (galactose-específica) reconhece o citoplasma neuronal e marca intensamente corpos amiláceos que ocorrem em abundância; ClaveLL (com elevada afinidade por N-acetil-D-glicosamina e glicoproteínas) reconhece intensamente células neuronais e corpos amiláceos e, mais importante, marca neurônios lesionados com emaranhados neurofibrilares ou com degeneração grânulovacuolar, degenerações que são típicas da doença de Alzheimer
APA, Harvard, Vancouver, ISO, and other styles
4

Correia, Jorge Luis Almeida. "Purificação, caracterização parcial e potencialidade biotecnológica de três lectinas de sementes de espécies de Leguminosae da subtribo Diocleinae." reponame:Repositório Institucional da UFC, 2015. http://www.repositorio.ufc.br/handle/riufc/18837.

Full text
Abstract:
CORREIA, Jorge Luis Almeida. Purificação, caracterização parcial e potencialidade biotecnológica de três lectinas de sementes de espécies de Leguminosae da subtribo Diocleinae. 2015. 101 f. Tese (Doutorado em biotecnologia)- Universidade Federal do Ceará, Fortaleza-CE, 2015.
Submitted by Elineudson Ribeiro (elineudsonr@gmail.com) on 2016-07-20T15:30:18Z No. of bitstreams: 1 2015_tese_jlacorreia.pdf: 12368047 bytes, checksum: 7bb605fd3353cb78f27981c1dea5ae71 (MD5)
Approved for entry into archive by José Jairo Viana de Sousa (jairo@ufc.br) on 2016-08-02T19:07:50Z (GMT) No. of bitstreams: 1 2015_tese_jlacorreia.pdf: 12368047 bytes, checksum: 7bb605fd3353cb78f27981c1dea5ae71 (MD5)
Made available in DSpace on 2016-08-02T19:07:50Z (GMT). No. of bitstreams: 1 2015_tese_jlacorreia.pdf: 12368047 bytes, checksum: 7bb605fd3353cb78f27981c1dea5ae71 (MD5) Previous issue date: 2015
Leguminosae is recognized by the large amount of isolated and characterized lectins, especially seeds. In this group stand out proteins extracted from species belonging to subtribe Diocleinae, the number of studies in different areas of knowledge. Lectins can be defined as proteins or glycoproteins which are not originated from a body's immune response and have the ability to recognize and bind reversibly to mono or oligosaccharides particular without, however, altering their chemical structures. Different works in our group are structurally haracterizing these proteins as well as elucidating some possible biotechnological applications for these molecules. In this sense, the objective of this study was to isolate and characterize lectins of different species of Leguminosae of Diocleinae subtribe and test them for toxicity to Artemia sp. naupilos, The effect on the smooth muscle of blood vessels and the detention lectin matrix agarose previously activated with cyanogenic bromide (CNBr). Were isolated and characterized the lectin Dioclea sclerocarpa, Dioclea lasiocarpa and Dioclea lasiophylla. Were also made circular dichroism studies on lectin Dioclea sclerocarpa and Dioclea lasiocarpa. The lectin Dioclea lasiophylla was tested against Artemia sp. order to assess their toxicity and was also immobilized on agarose matrix. We evaluated the effect of lectin Dioclea lasiocarpa in the smooth muscle of blood vessels. The knowledge gained from the three scientific articles published in this thesis is a major breakthrough in this promising field of study that has been continuously growing for biotechnological applications.
A família Leguminosae é reconhecida pela grande quantidade de lectinas isoladas e caracterizadas, especialmente de sementes. Neste grupo se destacam as proteínas extraídas de espécies pertencentes a subtribo Diocleinae, pela quantidade de estudos em diferentes áreas do conhecimento. Lectinas podem ser definidas como proteínas ou glicoproteínas que não são originadas a partir de uma resposta imunológica do organismo e possuem a capacidade de reconhecer e se ligar reversivelmente a mono ou oligossacarídeos específicos sem, no entanto, alterar suas estruturas químicas. Diferentes trabalhos no nosso grupo vêm caracterizando estruturalmente essas proteínas, bem como elucidando algumas possíveis aplicações biotecnológicas para essas moléculas. Neste sentido, o objetivo deste trabalho foi isolar e caracterizar lectinas de diferentes espécies de Leguminosae da subtribo Diocleinae e testa-las com relação à toxicidade para naupilos de Artemia sp., o efeito na musculatura lisa de vasos sanguíneos e a imobilização de lectina em matriz de agarose previamente ativada com brometo cianogênico (CNBr). Foram isoladas e caracterizadas as lectinas de Dioclea sclerocarpa, Dioclea lasiocarpa e Dioclea lasiophylla. Também foram feitos estudos de dicroísmo circular na lectina de Dioclea sclerocarpa e Dioclea lasiocarpa. A lectina de Dioclea lasiophylla foi testada contra Artemia sp.de forma a avaliar sua toxicidade e também foi imobilizada em matriz de agarose. Foi avaliado o efeito da lectina de Dioclea lasiocarpa na musculatura lisa de vasos sanguineos. O conhecimento acumulado a partir dos três artigos científicos publicados nesta tese constitui um grande avanço no neste campo promissor de estudo que vem em contínuo crescimento para aplicação biotecnológica.
APA, Harvard, Vancouver, ISO, and other styles
5

Colin, Sylvie. "Étude biochimique et spécifique d'une lectine extracellulaire impliquée dans la floculation de la levure kluyveromyces bulgaricus." Nancy 1, 1993. http://www.theses.fr/1993NAN10044.

Full text
Abstract:
K. Bulgaricus flocule en milieu enrichi en calcium. Ce phénomène est lie à l'excrétion d'une lectine spécifique du galactose (kb-ml). Le fait que le trifluoroperazine inhibe la floculation alors que l'ophioboline A n'a pas d'effet suggère qu'une protéine kinase indépendante de la calmoduline pourrait être impliquée dans le mécanisme de la floculation. Kb-ml présente deux formes moléculaires de 250 et 65 kda respectivement kb-mli est la forme tetramérique de kb-MLII. Les deux formes kb-MLI et kb-MLII agglutinent les hématies mais la première a une activité spécifique 6 fois supérieure à la seconde. L'association de kb-MLII pour former kb-MLI dépend de la concentration en protéine et seuls, les agents dénaturants (sds, urée) peuvent l'inhiber. La proline, la glycine et l'alanine représentent 60% de la partie peptidique des deux formes. La partie osidique (13%) est constituée de chaines n-oligomannosidiques. Les deux formes montrent la même microhétérogénéité avec un produit majeur de phi 4,5 et deux mineures de phi 3,9 et 4,9. Kb-MLII a deux sites fixateurs des sucres avec un ka de 1,12. 10#6 m##1 pour le 4-methylumbelliferyl-d-gal. Kb-MLI et kb-MLII reconnaissent les glycannes de type n-acetyllactosamine et la structure glcnac b1-2 man est la mieux reconnue. La déphosphorylation des mannoprotéines de la paroi de la levure kb stimule l'interaction de ces molécules avec kb-MLI et kb-MLII. Ces résultats suggèrent que l'antigène somatique (glcnaca1-2 man) de la levure est un site de reconnaissances pour cette lectine et que la phosphorylation de la surface cellulaire agit comme un modulateur de la floculation de k. Bulgaricus
APA, Harvard, Vancouver, ISO, and other styles
6

Andersson, Pontus. "Comparison of Lectins and their suitability in Lectin Affinity Chromatography for isolation of Glycoproteins." Thesis, Uppsala universitet, Institutionen för biologisk grundutbildning, 2020. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-417024.

Full text
Abstract:
Virtually all extracellular proteins in humans are glycoproteins and likewise are many biopharmaceuticals. The glycosylation is directly correlated to biological function and stability of these proteins. The ability to isolate glycoproteins is thus of great importance in many applications. The most common isolation method for glycoproteins is affinity chromatography using lectins, a ubiquitous and versatile group of carbohydrate-binding proteins. The lectin Concanavalin A (ConA) has long been used for this purpose but suffers from undesired leakage into the eluate, causing an inquiry of alternative chromatography ligands or optimization of the ConA resin.In this study, a total of 20 different lectins, including ConA, were evaluated and compared in terms of suitability as ligands in affinity chromatography for glycoprotein isolation. The lectins’ binding to glycoproteins were studied, mainly through microtiter plate binding assays using a monoclonal IgG1 antibody and Conalbumin (Ovotransferrin). Further, sugar-specificities and potential eluting sugars for the lectins were examined through inhibition with eight different carbohydrates. Additionally, the glycoprotein binding and leakage of ConA columns were examined, and a potential leakagereducing treatment of ConA resin evaluated.ConA was found to be superior in binding to the investigated glycoproteins but exhibited a limited binding when immobilized to an agarose resin. This discrepancy is likely a consequence of structurally hidden glycans on the used glycoproteins and requirements of long residence time when used in a chromatographic setting. Binding competition with several sugars were investigated with a similar microtiter plate binding assay. This method displayed potential to predict the behaviour of sugars and their suitability as eluting agents in a chromatography column. The best eluting sugar for ConA was showed to be methylmannoside, ideally in combination with methylglucoside. Lastly, evaluation of ConA columns with a crosslinking glutaraldehyde-treatment showed that the ConA ligand leakage may be significantly reduced, although further studies and optimizations are needed.This study thus presents a repertoire of lectins and their differences in terms of glycoprotein-binding and sugar-specificity, as well as evaluations of ConA columns’ efficiency and potential leakage-prevention.
APA, Harvard, Vancouver, ISO, and other styles
7

CrisÃstomo, ClÃbia Vieira. "PolissacarÃdeo endospÃrmico de Bauhinia pentandra: caracterizaÃÃo e estudo de interaÃÃo com lectinas." Universidade Federal do CearÃ, 2008. http://www.teses.ufc.br/tde_busca/arquivo.php?codArquivo=4498.

Full text
Abstract:
Conselho Nacional de Desenvolvimento CientÃfico e TecnolÃgico
Devido Ãs suas diferentes propriedades quÃmicas tais como capacidade de formar soluÃÃes viscosas ou gÃis em meio aquoso o isolamento e caracterizaÃÃo de galactomananas tÃm sido de grande importÃncia Nesse trabalho a galactomanana do endosperma da semente de Bauhinia pentandra foi isolada e caracterizada, apresentando-se homogÃnea por GPC Este polissacarideo foi demonstrado ser uma galactomanana clÃssica formada por uma cadeia linear de manose unidas por ligaÃÃes β(1-4) com substituiÃÃes de galactose em ligaÃÃo α(1-6) com uma proporÃÃo Man:Gal de 2 5.1 e viscosidade intrÃnseca em Ãgua de 10 1 dL/g A galactomanana foi avaliada quanto à capacidade de interagir com lectinas galactose ligante O polissacarÃdeo foi tratado com epicloridrina e o material obtido foi utilizado para a montagem de coluna cromatogrÃfica de afinidade Extratos ricos em lectinas de Artocarpus incisa Artocarpus integrifÃlia e Bauhinia pentandra foram aplicados e fraÃÃes lectinicas purificadas foram obtidas A capacidade da galactomanana de B. pentandra em reter a lectina (LBp) da mesma semente foi comparada com a matriz de galactomanana de Adenantera pavonina Caesalpinea pulcherrima Sophora japonica e com a matriz comercial Sepharose 4B Apesar da galactomanana de B. pentandra ter apresentado a menor capacidade de retenÃÃo frente Ãs demais, ela mostrou-se semelhante à matriz comercial sendo viÃvel a sua utilizaÃÃo
Due the chemicals properties diferences, such as the ability to make viscous solution or aqueous gels, the study of the galactomanans has been too important. In this study, the endospermic galactomannans from seeds of Bauhinia pentandra was isolated and partially characterized. This polysaccharide is a classical galalactomannan constituted by a linear chain of mannose linked by β(1-4) linkages with galactose substituintions linked by α(1-6) linkages, resulting in a Man:Gal ratio of 2.5:1, and water intrinsic viscosity equal to 10.1 dL/g. Galactomannan was evaluated in ability to interact with galactose-binding lectins. The polysaccharide was treated with epichlorohidrine and the material obtained was utilized to make the affinity chromatography matrix. Lectin-rich extracts from Artocarpus incisa, Artocarpus integrifolia and Bauhinia pentandra were applied and lectin fractions were obtained, thus, the affinity matrix showed to be efficient to isolate them. The retention capacity of the galactomannan from B. pentandra was compared with galactomannan matrix from Adenantera pavonina, Caesalpinea pulcherrima, Sophora japonica and commercial matrix of Sepharose 4B in regards to the isolation of the lectin from B. pentandra (LBp). Although the galactomannan matrix had been showed the smallest retention capacity in comparision with the others, it is equivalent to the commercial matrix, enabling your utilization
APA, Harvard, Vancouver, ISO, and other styles
8

Santori, Fabio. "Lectin affinity chromatography of monosaccharides." Thesis, University of Bath, 2002. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.760807.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Nascimento, Antônia Sâmia Fernandes do. "Lectines recombinantes d'algues rouges marines Hypnea musciformis (Wulfen) J.V. Lamouroux et Bryothamnion triquetrum (S.G. Gmelin) M. Howe : production hétérologue et caractérisation biochimique." Thesis, Grenoble, 2014. http://www.theses.fr/2014GRENV052/document.

Full text
Abstract:
Les gènes synthétiques des lectines des algues marines rouges Hypnea musciformis (HML) et Bryothamnion triquetrum (BTL) ont été clonés dans différents vecteurs et transformés dans plusieurs souches bactériennes d’expression. Les lectines recombinantes ont été obtenues dans la fraction soluble de cultures bactérienne dans les souches d’Escherichia coli Rosettagami 2 (DE3) pour rHML et BL21 (DE3) pour rBTL. Les tests d'hémagglutination ont montré que rHML et rBTL sont capables d’agglutiner les érythrocytes de lapin avec un bon pouvoir hémagglutinant mais seulement après traitement à la trysine et la papaine indiquant que leur ligands ne sont pas directement accessibles à la surface des hématies. Les propriétés hémagglutinantes de rHML et de rBTL confirment le repliement correct et l'état fonctionnel des protéines. La caractérisation de leur spécificité sur puces à sucres a montré une spécificité stricte de HML, BTL et rBTL pour les oligosaccharides complexes comportant la fucosylation (α1-6) du noyau, avec une préférence particulière pour les N-glycanes non bissectés, bi- et tri-antennés de chaîne courte. La présence d’acide sialique à l'extrémité non réductrice du glycane favorise la reconnaissance de ces glycanes. C'est la première caractérisation des lectines d’algues rouges par puce à sucres. Des expériences de STD-RMN menées sur BTL, ont montré son interaction avec un octasaccharide au niveau de noyau fucosylé (α1-6). L'activité toxique des lectines sauvages et recombinantes a été évaluée contre Artemia sp. et contre des cellules d'adénocarcinome du poumon (A549). Dans les essais de cytoxicité, HML, rHML, BTL et rBTL n’ont montré aucune toxicité contre Artemia sp. et seulement HML et rHML ont montré une cytotoxicité faibles contre les cellules d’adénocarcinome du poumon (A549). Le premier cristal de rBTL a été obtenu à l'aide d'un robot de cristallisation et diffractait à 15 Å
Synthetic genes from the red marine algae Hypnea musciformis (HML) and Bryothamnion triquetrum (rBTL) were cloned into different vectors and transformed into several bacterial expression strains. The recombinant lectins were obtained from the soluble fraction of bacterial cultures using Escherichia coli Rosettagami 2 (DE3) strain for rHML and E. coli BL21 (DE3) strain for rBTL. Haemagglutination tests showed that rHML and rBTL are able to agglutinate rabbit erythrocytes with strong haemagglutination activity only after treatment with papain and trysine indicating that their ligands are not directly accessible at the cell surface. The haemagglutinating properties of rHML and rBTL confirm the correct folding and functional state of the proteins. A study of the specificity of these lectins by glycan array was conducted. HML, BTL and rBTL showed a restricted specificity for complex N-glycans with core (α1-6) fucose. A more detailed analysis of the specificity of these lectins showed a preference for non bisecting N-glycans, bi- and tri-antennary branching sugars with short chains. Addition of Sialic acid at the non-reducing end of N-glycans favors their recognition by the lectins. This is the first characterization of lectins from red algae by glycan array. An interaction between BTL and a core (α1-6) fucosylated octasaccharides was also observed by STD-NMR. The toxic activity of wild and recombinant lectins were evaluated against Artemia sp. and the human lung adenocarcinoma cell line (A549). In cytotoxicity assays, HML, rHML, BTL and rBTL showed no toxicity against Artemia sp. Only HML and rHML showed a low cytotoxic activity against cell line (A549). The first crystal of rBTL was obtained in micro-scale level using a robot and diffracted at 15 Å
APA, Harvard, Vancouver, ISO, and other styles
10

Sicard, Delphine. "Caractérisation par microscopie à force atomique des arrangements protéine/sucre impliquant la lectine PA-IL de la bactérie pseudomonas aeruginosa." Phd thesis, Ecole Centrale de Lyon, 2012. http://tel.archives-ouvertes.fr/tel-00904559.

Full text
Abstract:
La bactérie Pseudomonas aeruginosa est un pathogène opportuniste responsable de graves infections chez les personnes affaiblies immunitairement. Présentant des souches résistantes aux antibiotiques, une nouvelle approche thérapeutique est en cours de développement avec pour objectif l'inhibition des facteurs de virulence de la bactérie. Lors de son processus d'infection, le pathogène utilise les lectines pour reconnaître et se lier de manière spécifique aux glycoconjugués des cellules-hôtes en formant une interaction lectine/glycoconjugué. Plus particulièrement, la lectine PA-IL, spécifique du galactose, a été étudiée. A l'aide de glycomimétique, il semble possible de bloquer l'action de la lectine en créant une interaction lectine/glycomimétique. Pour développer cette approche, de nombreux glycocluster sont donc été élaborés et leur affinité avec la lectine PA-IL a été évaluée par plusieurs méthodes de caractérisation (SPR, HIA, ELLA, puce à sucre,...).Dans ce projet de thèse, nous avons cherché à visualiser par microscopie à force atomique (AFM) l'arrangement des complexes lectine PA-IL/glycocluster formés pour trois glycoclusters différents. Nous avons ainsi pu montrer l'influence du cœur du glycocluster et des bras-espaceurs sur l'arrangement des complexes. Suivant le glycocluster, l'arrangement prend la forme de filaments 1D,de structures dentelées avec des bras sinueux ou encore de larges structures compactes. Dans le cas des filaments, la résolution de nos images AFM nous a permis d'identifier les lectines à l'intérieur même de la structure filaire. Nous avons aussi démontré, en observant les lectines seules, l'existence d'une interaction lectine/lectine. De plus, des expériences ont été menées pour déterminer les conditions expérimentales appropriées à leur observation à l'air et en milieu liquide.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Books on the topic "Lectin"

1

M, Rhodes Jonathan, and Milton Jeremy D, eds. Lectin methods and protocols. Totowa, N.J: Humana Press, 1998.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
2

J, Doyle Ronald, and Slifkin Malcolm, eds. Lectin-microorganism interactions. New York: M. Dekker, 1994.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
3

Rhodes, Jonathan M., and Jeremy D. Milton. Lectin Methods and Protocols. New Jersey: Humana Press, 1997. http://dx.doi.org/10.1385/0896033961.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Figura, L. O. Lectin methods and protocols. [Place of publication not identified]: Humana, 2010.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
5

Hirabayashi, Jun, ed. Lectin Purification and Analysis. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0430-4.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Franz, Hartmut, Ken-ichi Kasai, Jan Kocourek, Sjur Olsnes, and Leland M. Shannon, eds. Advances in Lectin Research. Berlin, Heidelberg: Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-662-11057-7.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Franz, Hartmut, Ken-ichi Kasai, Jan Kocourek, Sjur Olsnes, and Leland M. Shannon, eds. Advances in Lectin Research. Berlin, Heidelberg: Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-662-11060-7.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Franz, Hartmut, Ken-ichi Kasai, Jan Kocourek, Sjur Olsnes, and Leland M. Shannon, eds. Advances in Lectin Research. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-662-26751-6.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Yamasaki, Sho, ed. C-Type Lectin Receptors in Immunity. Tokyo: Springer Japan, 2016. http://dx.doi.org/10.1007/978-4-431-56015-9.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Brooks, S. A. Lectin histochemistry: A concise practical handbook. Oxford: BIOS Scientific in association with the Royal Microscopical Society, 1997.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Book chapters on the topic "Lectin"

1

Makkar, Harinder P. S., P. Siddhuraju, and Klaus Becker. "Phytohemagglutin/Lectin." In Plant Secondary Metabolites, 15–21. Totowa, NJ: Humana Press, 2007. http://dx.doi.org/10.1007/978-1-59745-425-4_4.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Vierbuchen, M. "Lectin Receptors." In Current Topics in Pathology, 271–361. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-75515-6_10.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Narayanan, Sahya, Akhila Raj Pallan, Akshay Balakrishnan, Eldho J. Paul, and Preetham Elumalai. "Animal Lectin." In Lectins, 89–106. Singapore: Springer Singapore, 2021. http://dx.doi.org/10.1007/978-981-16-7462-4_5.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Kim, Cheorl-Ho. "C-Type Lectin (C-Type Lectin Receptor)." In Glycobiology of Innate Immunology, 497–555. Singapore: Springer Singapore, 2022. http://dx.doi.org/10.1007/978-981-16-9081-5_8.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Sharon, N., and H. Lis. "Lectin resistant cells." In Lectins, 92–96. Dordrecht: Springer Netherlands, 1989. http://dx.doi.org/10.1007/978-94-011-4846-7_10.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Pérez, Serge, Alain Rivet, and Anne Imberty. "3D-Lectin Database." In Glycoscience: Biology and Medicine, 1–7. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54836-2_29-1.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Pérez, Serge, Alain Rivet, and Anne Imberty. "3D-Lectin Database." In Glycoscience: Biology and Medicine, 283–89. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54841-6_29.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Murphy, J. B., and M. E. Etzler. "Cloning Lectin Genes." In Lectins and Glycobiology, 447–57. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-77944-2_49.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Kobayashi, Yuka. "Lectin Affinity Electrophoresis." In Methods in Molecular Biology, 121–29. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-1292-6_11.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

O’Connor, Brendan F., Donal Monaghan, and Jonathan Cawley. "Lectin Affinity Chromatography." In Methods in Molecular Biology, 225–36. New York, NY: Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-3362-5_12.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "Lectin"

1

Scheefers, H., A. Kobus, and R. Geyer. "CARBOHYDRATE COMPOSITION AND LECTIN BINDING AFFINITIES OF HUMAN PLACENTAL TISSUE FACTOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643737.

Full text
Abstract:
Tissue factor (TF) is a widely distibuted membrane glycoprotein and the most potent trigger of bloodcoagulation. It serves as an essential cofactor for the activation of Factor IX and X by Factor Vll/VIIa.TF is a lipoprotein composed of a phospholipid portion and a glycosylated apoprotein (apo-TF). The procoagulant activity of bovine brain TF is inhibited bythe lectin Con A indicating that the carbohydrates of TF might play a functional role in its interactionwith Factor Vll/VIIa.In the present study apo-TF was purified from human placenta by repeated SDS-PAGE to a purity of 95%. The carbohydrates of apo-TF wereanalyzed by capillary gas- liquid-chromatography andmass-fragmentography. This analysis revealed that apo-TF contains about 16% (w/w) carbohydrate consistingof 50.4 mole% N-acetylglucosamine, 22.2 mole% mannose, 21.0 mole% galactose, 3.2 mole% fucose and 3.2 mole% N-acetylgalactosamine. Further information on the structure of the carbohydrate moieties of the apoTF was achieved by determining the binding affinities of the apo-TF to ten different lectins. For this purpose a semiquantitative spot lectino sorbent assaywas developed. This assay is based on the detection of peroxidase-labeled lectins after being bound to the carbohydrate moieties of apo-TF adsorbed onto a nitrocellulose membrane. Human placental apo-TF showed the strongest affinity to wheat germ agglutinin which specifically binds to N-acetylglucosamine and sialic acid residues.In contrast to bovine brain apo-TF, human placental apo-TF only weakly interacted with Con A, which is known to recognize mannosyl residues in mannose-rich, hybrid- and biantennary glycans,but not in tri- or tetraantennary oligosaccharides of the complex type. From the carbohydrate constituent analysis and from the lectin binding studies it can be concluded that human placental apo-TF carriesabout four N-linked higher branched oligosaccharide chains.
APA, Harvard, Vancouver, ISO, and other styles
2

Wang, Deyu, Duxiao Jiang, and Chunwei Yuan. "Spectral characters of lectin saccharide interaction." In International Symposium on Biomedical Optics, edited by Qingming Luo, Britton Chance, Lihong V. Wang, and Steven L. Jacques. SPIE, 1999. http://dx.doi.org/10.1117/12.364383.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Cao, Xiaohong, Minghui Zhou, Chunling Wang, Lihua Hou, and Linye Chen. "Immunomodulatory effect of lectin from Musca domestic pupa on immunosuppressive mice: Effect of lectin on immunosuppressive mice." In 2011 International Conference on Human Health and Biomedical Engineering (HHBE). IEEE, 2011. http://dx.doi.org/10.1109/hhbe.2011.6027885.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Abd Rahman, Siti Fatimah, Mohd Khairuddin Md Arshad, Subash C. B. Gopinath, Mohamad Faris Mohamad Fathil, Frederic Sarry, and Mohammad Nuzaihan Md Nor. "Impedimetric Lectin Biosensor for Prostate Cancer Detection." In 2021 IEEE International Conference on Sensors and Nanotechnology (SENNANO). IEEE, 2021. http://dx.doi.org/10.1109/sennano51750.2021.9642659.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Lian, E. C. Y., and F. A. Siddigui. "BINDING OF 37-DKa PLATELET AGGLUTINATING PROTEIN TO HUMAN PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643976.

Full text
Abstract:
We have previously reported the purification of a 37-KDa platelet agglutinating protein (PAP p37) from the plasma of a patient with thrombotic thrombocytopenic purpura. using 125I-labeled p37, the properties of its binding to platelets were studied. The binding of p37 to washed human platelets from 4 normal subjects and two TTP patients after recovery was specific, concentration dependent and saturable. The Scatchard analysis revealed that the binding sites for p37 was about 100,000 per platelet with a dissociation constant of 48 × 10−9 M. The binding of p37 to erythrocytes was very little and non-specific. Stimulation of platelets by thrombin or ADP did not have any effect on the binding of p37 to platelets. The monoclonal antibodies to platelet GP lb (6D1) and GP Ilb-llla (10E5)(A gift of Dr. Barry coller) did not inhibit the binding of p37 to platelets. Fibrinogen (1 mg/ml) and FVIII/vWF (250 ug/ml) reduced the binding slightly. The polyclonal antibodies to p37 as well as concanavalin-A inhibited the binding of p37 to platelets through their direct interaction with p37. Other lectins such as phytohemagglutinin, potato lectin and helix pomatia lectin did not have any effect. At 40 mM, sialic acid, α-D-(+)-glucose, D-(+)-mannose and D-fructose caused 91%,44%,79%, and 63% inhibition of p37 binding respectively. D-(+)-galactose did not interfere with the binding. It is concluded that p37 binds to platelets on the sites other than GP lb and Gp IIb-IIIa and its binding to platelets is inhibited by certain sugars.
APA, Harvard, Vancouver, ISO, and other styles
6

S. Silva, M. Luísa. "Detection of cancer-associated glycobiomarkers using lectin-based biosensors." In 5th International Electronic Conference on Medicinal Chemistry. Basel, Switzerland: MDPI, 2019. http://dx.doi.org/10.3390/ecmc2019-06280.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

McClure, J., N. Ghasemi, RW Stoddart, and SF McClure. "THU0070 Immunohistological and lectin histochemical studies of sternoclavicular amyloidosis." In Annual European Congress of Rheumatology, Annals of the rheumatic diseases ARD July 2001. BMJ Publishing Group Ltd and European League Against Rheumatism, 2001. http://dx.doi.org/10.1136/annrheumdis-2001.924.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Helmholz, Heike, Peter Thiesen, and Bernd Niemeyer. "SILICA- AND POLYMER-BASED LECTIN ADSORBENTS FOR GLYCOCONJUGATE SEPARATION." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.390.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Hwa, Kuo-Yuan, An-Na Chen, Shuen-Iu Hung, Alice Chien Chang, and Han-Chi Chang. "BIOCHEMICAL ANALYSIS ON A NOVEL MAMMALIAN LECTIN YM-1." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.520.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Santos, Beate S., Patricia M. A. de Farias, Frederico D. de Menezes, Ricardo de C. Ferreira, Severino A. Junior, Regina C. B. Q. Figueiredo, and Eduardo I. C. Beltrão. "Lectin functionalized quantum dots for recognition of mammary tumors." In Biomedical Optics 2006, edited by Marek Osinski, Kenji Yamamoto, and Thomas M. Jovin. SPIE, 2006. http://dx.doi.org/10.1117/12.646819.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Reports on the topic "Lectin"

1

Fluhr, Robert, and Maor Bar-Peled. Novel Lectin Controls Wound-responses in Arabidopsis. United States Department of Agriculture, January 2012. http://dx.doi.org/10.32747/2012.7697123.bard.

Full text
Abstract:
Innate immune responses in animals and plants involve receptors that recognize microbe-associated molecules. In plants, one set of this defense system is characterized by large families of TIR–nucleotide binding site–leucine-rich repeat (TIR-NBS-LRR) resistance genes. The direct interaction between plant proteins harboring the TIR domain with proteins that transmit and facilitate a signaling pathway has yet to be shown. The Arabidopsis genome encodes TIR-domain containing genes that lack NBS and LRR whose functions are unknown. Here we investigated the functional role of such protein, TLW1 (TIR LECTIN WOUNDRESPONSIVE1). The TLW1 gene encodes a protein with two domains: a TIR domain linked to a lectin-containing domain. Our specific aim in this proposal was to examine the ramifications of the TL1-glycan interaction by; A) The functional characterization of TL1 activity in the context of plant wound response and B) Examine the hypothesis that wounding induced specific polysaccharides and examine them as candidates for TL-1 interactive glycan compounds. The Weizmann group showed TLW1 transcripts are rapidly induced by wounding in a JA-independent pathway and T-DNA-tagged tlw1 mutants that lack TLW1 transcripts, fail to initiate the full systemic wound response. Transcriptome methodology analysis was set up and transcriptome analyses indicates a two-fold reduced level of JA-responsive but not JA-independent transcripts. The TIR domain of TLW1 was found to interact directly with the KAT2/PED1 gene product responsible for the final b-oxidation steps in peroxisomal-basedJA biosynthesis. To identify potential binding target(s) of TL1 in plant wound response, the CCRC group first expressed recombinant TL1 in bacterial cells and optimized conditions for the protein expression. TL1 was most highly expressed in ArcticExpress cell line. Different types of extraction buffers and extraction methods were used to prepare plant extracts for TL1 binding assay. Optimized condition for glycan labeling was determined, and 2-aminobenzamide was used to label plant extracts. Sensitivity of MALDI and LC-MS using standard glycans. THAP (2,4,6- Trihydroxyacetophenone) showed minimal background peaks at positive mode of MALDI, however, it was insensitive with a minimum detection level of 100 ng. Using LC-MS, sensitivity was highly increased enough to detect 30 pmol concentration. However, patterns of total glycans displayed no significant difference between different extraction conditions when samples were separated with Dionex ICS-2000 ion chromatography system. Transgenic plants over-expressing lectin domains were generated to obtain active lectin domain in plant cells. Insertion of the overexpression construct into the plant genome was confirmed by antibiotic selection and genomic DNA PCR. However, RT-PCR analysis was not able to detect increased level of the transcripts. Binding ability of azelaic acid to recombinant TL1. Azelaic acid was detected in GST-TL1 elution fraction, however, DHB matrix has the same mass in background signals, which needs to be further tested on other matrices. The major findings showed the importance of TLW1 in regulating wound response. The findings demonstrate completely novel and unexpected TIR domain interactions and reveal a control nexus and mechanism that contributes to the propagation of wound responses in Arabidopsis. The implications are to our understanding of the function of TIR domains and to the notion that early molecular events occur systemically within minutes of a plant sustaining a wound. A WEB site (http://genome.weizmann.ac.il/hormonometer/) was set up that enables scientists to interact with a collated plant hormone database.
APA, Harvard, Vancouver, ISO, and other styles
2

Kraybill, William H. Lectin Enzyme Assay Detection of Viruses, Tissue Culture, and a Mycotoxin Simulant. Fort Belvoir, VA: Defense Technical Information Center, September 1988. http://dx.doi.org/10.21236/ada276469.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Braunschweig, Adam B., Shudan Bian, and Han Xu. Carbohydrate Nanotechnology: Hierarchical Assemblies and Information Processing from Oligosaccharide-Synthetic Lectin Host-Guest. Fort Belvoir, VA: Defense Technical Information Center, September 2014. http://dx.doi.org/10.21236/ada612784.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Wang, Xin. Synthesis and Characterization of Glyconanomaterials, and Their Applications in Studying Carbohydrate-Lectin Interactions. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.626.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Deutscher, Susan. Radiolabeled Peptide Scaffolds for PET/SPECT - Optical in Vivo Imaging of Carbohydrate-Lectin Interactions. Office of Scientific and Technical Information (OSTI), September 2014. http://dx.doi.org/10.2172/1158790.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Glazer, Itamar, Randy Gaugler, Yitzhak Spiegel, and Edwin Lewis. Host Adaptation in Entomopathogenic Nematodes: An Approach to Enhancing Biological Control Potential. United States Department of Agriculture, April 1996. http://dx.doi.org/10.32747/1996.7613023.bard.

Full text
Abstract:
The overall objective of our research was to develop methods to match species of entomopathogenic nematodes against the insect pests which they would be best adapted to control. The underlying hypothesis for this work was that entomopathogenic nematodes should be most effective when used against insect species to which they are naturally adapted to parasitize. Toward this end, we undertook a number of related studies focusing primarily on nematode foraging strategies. We found that foraging strategies affected host associations directly and indirectly. Nematodes' responses to host cues, and the role of their sensory organs based on lectin binding, led to new approaches to determining host range for these parasites. Based on this work, we developed a laboratory bioassay of host recognition behavior designed to predict field results. We also determined that nematodes that forage in a stationary manner (ambushers) have a slower metabolic rate than do active forgers (cruisers), thus their infective stage juveniles are longer lived. This study helps predict the duration of field activity after application and may partially explain field distributions of natural populations of entomopathogenic nematodes. The common thread linking all of these studies was that they led to a deeper understanding of the associations between entomopathogenic nematodes and insects as hosts.
APA, Harvard, Vancouver, ISO, and other styles
7

Thompson, Paul R., and John J. Lavigne. Synthetic Lectins: New Tools for Detection and Management of Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, August 2014. http://dx.doi.org/10.21236/ada612862.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Lavigne, John J. Synthetic Lectins: New Tools for Detection and Management of Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, August 2013. http://dx.doi.org/10.21236/ada591012.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Zhang, Shu, Tong Wang, and Donald C. Beitz. Soy Lecithin but Not Egg Lecithin Decreased the Plasma Cholesterol Concentration in Golden Syrian Hamsters. Ames (Iowa): Iowa State University, January 2006. http://dx.doi.org/10.31274/ans_air-180814-128.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Sharon, Nathan, and Maarten Chrispeels. Improvement of the Nutritional Value of Legume Storage Proteins by Genetic Engineering: Studies with Legume Lectins. United States Department of Agriculture, October 1991. http://dx.doi.org/10.32747/1991.7604278.bard.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'Lectin' for particular source types:
Journal articles Dissertations / Theses Books
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography