Literatura académica sobre el tema "Lectins"
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Artículos de revistas sobre el tema "Lectins"
Ogilvie, Mary L., JoAnn Wilson Byl y T. Kent Gartner. "Platelet Aggregation Is Stimulated by Lactose-lnhibitable Snake Venom Lectins". Thrombosis and Haemostasis 62, n.º 02 (1989): 704–7. http://dx.doi.org/10.1055/s-0038-1646887.
Texto completoKothari, Sajani, Rebecca Heineman y 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, n.º 7 (17 de julio de 2023): 1–10. http://dx.doi.org/10.26685/urncst.490.
Texto completoBonnardel, François, Julien Mariethoz, Serge Pérez, Anne Imberty y Frédérique Lisacek. "LectomeXplore, an update of UniLectin for the discovery of carbohydrate-binding proteins based on a new lectin classification". Nucleic Acids Research 49, n.º D1 (11 de noviembre de 2020): D1548—D1554. http://dx.doi.org/10.1093/nar/gkaa1019.
Texto completoLakhtin, M., V. Lakhtin, V. Alyoshkin y S. Afanasyev. "Lectins of beneficial microbes: system organisation, functioning and functional superfamily". Beneficial Microbes 2, n.º 2 (1 de junio de 2011): 155–65. http://dx.doi.org/10.3920/bm2010.0014.
Texto completoMelgarejo, Luz Marina, Nohora Vega y 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, n.º 3 (septiembre de 2005): 315–24. http://dx.doi.org/10.1590/s1677-04202005000300006.
Texto completoVan Holle, Sofie y Els J. M. Van Damme. "Signaling through plant lectins: modulation of plant immunity and beyond". Biochemical Society Transactions 46, n.º 2 (22 de febrero de 2018): 217–33. http://dx.doi.org/10.1042/bst20170371.
Texto completoMewe, Marco, Denis Tielker, Robert Schönberg, Melitta Schachner, Karl-Erich Jaeger y Udo Schumacher. "Pseudomonas aeruginosa lectins I and II and their interaction with human airway cilia". Journal of Laryngology & Otology 119, n.º 8 (agosto de 2005): 595–99. http://dx.doi.org/10.1258/0022215054516313.
Texto completoLesman-Movshovich, Efrat, Batia Lerrer y Nechama Gilboa-Garber. "Blocking ofPseudomonas aeruginosalectins by human milk glycans". Canadian Journal of Microbiology 49, n.º 3 (1 de marzo de 2003): 230–35. http://dx.doi.org/10.1139/w03-027.
Texto completoCoelho, Luana Cassandra Breitenbach Barroso, Priscila Marcelino dos Santos Silva, Vera Lúcia de Menezes Lima, Emmanuel Viana Pontual, Patrícia Maria Guedes Paiva, Thiago Henrique Napoleão y Maria Tereza dos Santos Correia. "Lectins, Interconnecting Proteins with Biotechnological/Pharmacological and Therapeutic Applications". Evidence-Based Complementary and Alternative Medicine 2017 (2017): 1–22. http://dx.doi.org/10.1155/2017/1594074.
Texto completoGerhardus, M. J. T., J. M. C. Baggen, W. P. W. Van Der Knaap y T. Sminia. "Analysis of surface carbohydrates of Trichobilharzia ocellata miracidia and sporocysts using lectin binding techniques". Parasitology 103, n.º 1 (agosto de 1991): 51–59. http://dx.doi.org/10.1017/s003118200005928x.
Texto completoTesis sobre el tema "Lectins"
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/.
Texto completoRecently 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
Silva, Luana Maria Castelo Melo. "Efeito da lectina da alga marinha vermelha Pterocladiella capillace em feridas limpas induzidas em ratos". reponame:Repositório Institucional da UFC, 2012. http://www.repositorio.ufc.br/handle/riufc/18834.
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Based on the need for new formulations that are more efficient and on the properties provided by molecules derived from seaweed, it is believed that these can be effective in healing process. The lectin from the red seaweed Pterocladiella capillacea (PcL) and the polysaccharides of red algae Solieria filiformis (SfP) were initially analyzed in toxicity testing. PcL was applied to the paw edema test followed by measurement of myeloperoxidase (MPO). We evaluated the effect of the seaweed Pterocladiella capillacea lectin (PcL) and algal polysaccharides Solieria filiformis (SfP) in healing wounds in rats induced. Both molecules were submitted to microbiological tests and assayed for the effect on wound healing in wounds clean induced on the back of rats. SfP was used as a possible vehicle for the administration of PcL and compared to Carbopol 940 (C). The gels (0.9%) were analyzed rheological and then applied to the lesions during a treatment period of 10 days, using kollagenase ® as control. The healing process was evaluated on the size of the wounds, levels of MPO and histological analysis. The molecule SfP and PcL is not toxic for the parameters of body weight, organ and biochemical measurements. However, the histological analysis showed minor changes in liver and kidney. PcL (1, 3 and 9 mg / kg, i.v) reduced the edema induced by carrageenan and its inhibitor when administered with mucin was not possible to check the reduction of edema which was confirmed by measurement of MPO. The two molecules were used in microbiological assays and not inhibit growth of any microorganism tested and unable to use SfP as carbon source. The rheological analysis showed that the SfP used in the formulation of the gels (PcL+SfP and SfP) had the characteristic of a pseudoplastic. Macroscopic analysis of wounds showed a reduction in lesion area in the animals treated with PCL, PCL+SfP, PCL+C (53.5 and 60% respectively) on the sixth day of administration. In histological analysis, there was no severe inflammatory infiltrate in the tissues obtained until 4th day of administration of the gels (PcL and PcL+SfP, PcL+C) and Kollagenase® (positive control). On day 6, the untreated animals and those treated only with SfP showed inflammatory infiltrate. The measurement of MPO showed a reduction in the inflammatory process in the samples containing PcL, whose results corroborate the histological analysis. In conclusion, PcL aid in wound repair, suggesting its use as a possible future tool for the treatment of lesions. The biological and pharmacological role of lectins and polysaccharides of seaweed is part of a study area little explored, where a lot of knowledge should be invested since these biomolecules can be promising for the pharmaceutical industry.
Com base na necessidade de obter novas formulações mais eficientes e diante das propriedades apresentadas pelas moléculas oriundas de algas marinhas, acredita-se que estas possam ser eficazes no processo de cicatrização. A lectina da alga marinha vermelha Pterocladiella capillacea (PcL) e os polissacarídeos da alga vermelha Solieria filiformis (SfP) inicialmente foram analisados em ensaio de toxicidade. PcL foi aplicada no ensaio do edema de pata seguido da dosagem de mieloperoxidase (MPO). Avaliou-se o efeito da lectina da alga Pterocladiella capillacea (PcL) e os polissacarídeos das algas Solieria filiformis (SfP) na cicatrização de feridas induzidas em ratos. Ambas as moléculas foram submetidas a ensaios microbiológicos e analisadas quanto ao efeito no processo de cicatrização em feridas limpas induzidas no dorso de ratos. SfP foi utilizado como um possível veículo para a administração de PcL e comparado ao Carbopol 940 (C). Os géis (0,9%) foram submetidos a análise reológica e então aplicados nas lesões durante um período de tratamento de 10 (dez) dias, utilizando kollagenase® como controle. O processo de cicatrização foi avaliado quanto ao tamanho das feridas, dosagem de MPO e análise histológica. PcL e SfP não demonstraram toxicidade quanto aos parâmetros de peso corpóreo, órgãos e dosagens bioquímicas. Entretanto a análise histológica mostrou pequenas alterações no fígado e rim. PcL (1, 3 e 9 mg/kg, i.v.) reduziu o edema induzido por carragenana e quando administrada com seu inibidor mucina não foi possível verificar a redução do edema o qual foi confirmado pela dosagem de MPO. As duas moléculas foram aplicadas em ensaios microbiológicos e não inibiram o crescimento de nenhum micro-organismo testado, os quais também não foram capazes de utilizar SfP como fonte de carbono. A análise reológica mostrou que os SfP utilizados na formulação dos géis (PcL+SfP e SfP) apresentaram a característica de um pseudoplástico. A análise macroscópica das feridas mostrou uma redução da área da lesão nos animais tratados com PcL+SfP e PcL+C (53,5 e 60%, respectivamente) no sexto dia de administração. Na análise histológica, não foi observado infiltrado inflamatório acentuado nos tecidos obtidos até o 4º dia da administração dos géis (PcL+SfP e PcL+C) e Kollagenase® (controle positivo). No 6º dia, os animais não tratados e os tratados apenas com SfP mostraram infiltrado inflamatório. A dosagem de MPO demonstrou redução no processo inflamatório nas amostras contendo PcL, cujo resultado corrobora com a análise histológica. Em conclusão, PcL auxiliou no reparo de feridas, sugerindo seu uso futuro como uma possível ferramenta para o tratamento de lesões. O papel biológico e farmacológico das lectinas e polissacarídeos de algas marinhas faz parte de uma área de estudos ainda pouco explorada, onde muito conhecimento deverá ser investido visto que estas biomoléculas podem ser promissoras para a indústria farmacêutica.
Oliveira, Wilian Rosário de. "Lectinas de Crotalaria spectabilis R.: isolamento, purificação e atividade aglutinante em Leptospira biflexa (saprófita) e L. interrogans (patogênica)". Instituto de Ciências da Saúde, 2014. http://repositorio.ufba.br/ri/handle/ri/23507.
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CAPES
Lectinas são proteínas que se ligam especificamente a resíduos de açúcar e estão envolvidas no processo de reconhecimento celular e sinalização em diversas vias metabólicas. O objetivo deste estudo foi isolar, purificar e investigar a atividade biológica das lectinas de Crotalaria spectabilis R. quanto a sua capacidade de hemaglutinação e aglutinação das linhagens bacterianas: Leptospira biflexa e L. interrogans. Para extração das proteínas, as sementes foram moídas e suas células lisadas em solução NaCl 0,15 M. Após essa etapa, as proteínas foram precipitadas com acetona e sulfato de amônio, dialisadas, liofilizadas e purificadas por cromatografia de filtração e troca iônica. A quantificação proteica foi realizada pelo método de Bradford e o perfil eletroforético obtido por SDS-PAGE. Para testar a atividade biológica das lectinas foram utilizados ensaios de hemaglutinação bem como de aglutinação das linhagens bacterianas. Em nossos resultados, o método de precipitação proteica por acetona resultou em maior extração quando comparado ao método por sulfato de amônio. A lectina de C. spectabilis R. apresentou um peso molecular de 30 kDa e os ensaios de hemaglutinação foram positivos para a proteína. Assim, concluimos que nas sementes de C. spectabilis R. existem lectinas com capacidade de reconhecer receptores presentes na membrana de eritrócitos humanos e promover aglutinação celular. Por fim, as lectinas da planta C. spectabilis R. também foram capazes de aglutinar L. interrogans e L. biflexa, sendo esta reposta mais acentuada na linhagem patogênica.
Lectins are proteins that bind carbohydrate residues with affinity and are involved in the process of cell recognition and signaling in different metabolic pathways. The aim of this study was to isolate, purify and investigate the biological activity of the Crotalaria spectabilis R. lectins in terms of hemagglutination and agglutination capacity of the bacterial strains: Leptospira biflexa and L. interrogans. For protein extraction, the seeds were milled and their cells lysed in 0,15 M NaCl solution. After this step, the proteins were precipitated with acetone and ammonium sulfate, dialyzed, lyophilized and purified by filtration chromatography and ion exchange, respectively. Protein quantification was performed by the Bradford method and the electrophoretic profile by SDS-PAGE. For testing the biological activities of lectins, hemagglutination assays were used as well agglutination of the bacterial strains. In our results, protein precipitation method by acetone resulted in higher yield when compared to ammonium sulfate. The C. spectabilis R. lectin presented a molecular weight of 30 kDa and the hemagglutination assays were positives for the protein. Thus, we conclude that in the C. spectabilis R. seeds there are lectins with capacity to recognize receptors present in the human erythrocytes membrane and to promote cell agglutination. At last, the seed lectin C. spectabilis R. was also able to agglutinate L. interrogans and L. biflexa, this response being stronger in the pathogenic strain.
Bibi, Rashda. "Synthèse de nouveaux dérivés osidiques pour le ciblage de lectines originales". Thesis, Montpellier, Ecole nationale supérieure de chimie, 2012. http://www.theses.fr/2012ENCM0002.
Texto completoRhamnose binding lectines were discovered as new class of lectines in 1990's. Most of these lectines has been isolated from aquatic animals. It was discovered in 1991 that rhamnose specific receptors may be present in human skin while studying the interaction between liposomes incorating synthesitic glycoproteins and keratinocytes. We have synthesized new derivatives of rhamnose to target these lectines
Santos, Adriano dos [UNESP]. "Estudo da afinidade das proteínas rTgMIC1 e rTgMIC4 da Toxoplasma gondii com fetuína e asialofetuína utilizando técnica piezelétrica". Universidade Estadual Paulista (UNESP), 2012. http://hdl.handle.net/11449/92055.
Texto completoCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
As proteínas de micronema TgMIC1 e TgMIC4 (TgMICs) da Toxoplasma gondii fazem parte de um complexo proteico localizado na superfície do parasita responsável pelo processo de adesão e invasão celular. Os objetivos desse trabalho foram estudar dispositivos piezelétricos contendo em cada um, uma das MICs recombinantes (rTgMIC1 ou rTgMIC4) e utilizá‐los na determinação das constantes de afinidade entre elas com a fetuína e asialofetuína, empregando o modelo da Isoterma de Langmuir. Os dispositivos foram desenvolvidos por meio a abordagem de monocamadas automontadas (SAM) mista de tióis, utilizando solução etanólica contendo 2,5 mM de ácido 11‐mercaptoundecanóico (11‐MUA) e 7,5 mM de 6‐mercapto‐1‐hexanol (C6OH). A formação da SAM, realizada em temperatura ambiente por 12 h, foi monitorada pela técnica de Microbalança a Cristal de Quartzo com Fator Dissipativo (QCM‐D) e voltametria cíclica utilizando o par redox [FeII(CN)6]4‐/ FeIII(CN)6]3‐. Os resultados obtidos por ambas as técnicas evidenciaram a formação de SAM rígida e de elevado grau de cobertura superficial após cinética lenta em que processos de adsorção e organização dos tióis ocorreram simultaneamente. Para a imobilização das rTgMICs, solução aquosa contendo 10 mM de EDC (N‐etil‐N‐(dimetilaminopropil) carbodiimida) e 20 mM de NHS (N‐hidroxisuccinimida) foi utilizada para a ativação dos grupos carboxílicos presentes na SAM por 2 h, e o processo acompanhado por QCM‐D apresentou resultados compatíveis com aqueles encontrados na literatura. Pela mesma técnica, foi possível verificar que ambas as rTgMICs se imobilizam sobre o cristal de quartzo após sua incubação com solução 0,15 mg/mL de cada rTgMIC em tampão Tris‐HCl contendo 200 mM de NaCl...
The Toxoplasma gondii micronemal proteins TgMIC1 and TgMIC4 (TgMICs) are part of a protein complex located on the surface of the parasite responsible for the process of cellular adhesion and invasion. The goal of the present work was to study a piezoelectric device containing the recombinant MICs (rTgMIC1 or rTgMIC4) and use it in determining the affinity constants between the MICs with fetuin and asialofetuin, employing the Langmuir isotherm model. The devices were developed using the approach of self‐assembled monolayer (SAM) in ethanolic solution containing 2.5 mM of 11‐mercaptoundecanoic acid (11‐MUA) and 7.5 mM of 6‐mercaptohexanol (C6OH). The SAM formation, held at room temperature for 12 h, was monitored by the Quartz Crystal Microbalance technique with Dissipative Factor (QCM‐D) and cyclic voltammetry using the redox couple [FeII(CN)6]4‐/FeIII(CN) 6]3‐. The results obtained from both techniques showed the formation of a rigid and high surface degree coverage SAM after a slow kinetic process in which adsorption and organization of the thiols occur simultaneously. For the immobilization of rTgMICs, aqueous solution containing 10 mM EDC N‐ethyl‐N‐(dimethylaminopropyl) carbodiimide and 20 mM NHS (N‐hydroxysuccinimide) was used for 2 h, and the process followed by QCM‐D was consistent with those found in the literature. By the same technique it was found that both rTgMICs are immobilized on the quartz crystal after incubation whit solution 0.15 mg/mL of each rTgMIC in Tris‐HCl containing 200 mM NaCl (pH 8.0) for 2 h. Unlike the functionalization of the quartz crystal rTgMIC4, remaining adsorption sites were observed in the process using the rTgMIC1, wherein the blocking step using 0.1% gelatin solution for 2 h was required. Throughout the QCM‐D technique it was possible... (Complete abstract click electronic access below)
Santos, Adriano dos. "Estudo da afinidade das proteínas "rTgMIC1" e "rTgMIC4" da Toxoplasma gondii com fetuína e asialofetuína utilizando técnica piezelétrica /". Araraquara : [s.n.], 2012. http://hdl.handle.net/11449/92055.
Texto completoBanca: Emanuel Carrilho
Banca: Maria Cristina Roque Antunes Barreira
Resumo: As proteínas de micronema TgMIC1 e TgMIC4 (TgMICs) da Toxoplasma gondii fazem parte de um complexo proteico localizado na superfície do parasita responsável pelo processo de adesão e invasão celular. Os objetivos desse trabalho foram estudar dispositivos piezelétricos contendo em cada um, uma das MICs recombinantes (rTgMIC1 ou rTgMIC4) e utilizá‐los na determinação das constantes de afinidade entre elas com a fetuína e asialofetuína, empregando o modelo da Isoterma de Langmuir. Os dispositivos foram desenvolvidos por meio a abordagem de monocamadas automontadas (SAM) mista de tióis, utilizando solução etanólica contendo 2,5 mM de ácido 11‐mercaptoundecanóico (11‐MUA) e 7,5 mM de 6‐mercapto‐1‐hexanol (C6OH). A formação da SAM, realizada em temperatura ambiente por 12 h, foi monitorada pela técnica de Microbalança a Cristal de Quartzo com Fator Dissipativo (QCM‐D) e voltametria cíclica utilizando o par redox [FeII(CN)6]4‐/ FeIII(CN)6]3‐. Os resultados obtidos por ambas as técnicas evidenciaram a formação de SAM rígida e de elevado grau de cobertura superficial após cinética lenta em que processos de adsorção e organização dos tióis ocorreram simultaneamente. Para a imobilização das rTgMICs, solução aquosa contendo 10 mM de EDC (N‐etil‐N‐(dimetilaminopropil) carbodiimida) e 20 mM de NHS (N‐hidroxisuccinimida) foi utilizada para a ativação dos grupos carboxílicos presentes na SAM por 2 h, e o processo acompanhado por QCM‐D apresentou resultados compatíveis com aqueles encontrados na literatura. Pela mesma técnica, foi possível verificar que ambas as rTgMICs se imobilizam sobre o cristal de quartzo após sua incubação com solução 0,15 mg/mL de cada rTgMIC em tampão Tris‐HCl contendo 200 mM de NaCl... (Resumo completo, clicar acesso eletrônico abaixo)
Abstract: The Toxoplasma gondii micronemal proteins TgMIC1 and TgMIC4 (TgMICs) are part of a protein complex located on the surface of the parasite responsible for the process of cellular adhesion and invasion. The goal of the present work was to study a piezoelectric device containing the recombinant MICs (rTgMIC1 or rTgMIC4) and use it in determining the affinity constants between the MICs with fetuin and asialofetuin, employing the Langmuir isotherm model. The devices were developed using the approach of self‐assembled monolayer (SAM) in ethanolic solution containing 2.5 mM of 11‐mercaptoundecanoic acid (11‐MUA) and 7.5 mM of 6‐mercaptohexanol (C6OH). The SAM formation, held at room temperature for 12 h, was monitored by the Quartz Crystal Microbalance technique with Dissipative Factor (QCM‐D) and cyclic voltammetry using the redox couple [FeII(CN)6]4‐/FeIII(CN) 6]3‐. The results obtained from both techniques showed the formation of a rigid and high surface degree coverage SAM after a slow kinetic process in which adsorption and organization of the thiols occur simultaneously. For the immobilization of rTgMICs, aqueous solution containing 10 mM EDC N‐ethyl‐N‐(dimethylaminopropyl) carbodiimide and 20 mM NHS (N‐hydroxysuccinimide) was used for 2 h, and the process followed by QCM‐D was consistent with those found in the literature. By the same technique it was found that both rTgMICs are immobilized on the quartz crystal after incubation whit solution 0.15 mg/mL of each rTgMIC in Tris‐HCl containing 200 mM NaCl (pH 8.0) for 2 h. Unlike the functionalization of the quartz crystal rTgMIC4, remaining adsorption sites were observed in the process using the rTgMIC1, wherein the blocking step using 0.1% gelatin solution for 2 h was required. Throughout the QCM‐D technique it was possible... (Complete abstract click electronic access below)
Mestre
Destecroix, Harry. "Anthracene based synthetic lectins". Thesis, University of Bristol, 2015. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.682557.
Texto completoAndersson, 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.
Texto completoSousa, Bruno Lopes de. "CaracterizaÃÃo estrutural das formas silvestre e recombinante de uma lectina de sementes de Vatairea macrocarpa Benth e anÃlise das suas bases moleculares de ligaÃÃo ao antÃgeno Tn". Universidade Federal do CearÃ, 2014. http://www.teses.ufc.br/tde_busca/arquivo.php?codArquivo=13196.
Texto completoAs lectinas consitem em uma classe diversificada de proteÃnas, capazes de reconhecer estruturas glicÃdicas de forma reversÃvel e com alta especificidade, no entanto sem alterar suas estruturas quÃmicas, participando de vÃrios processos celulares importantes. Dentre as diferentes famÃlias de lectinas, as isoladas a partir de leguminosas sÃo as mais extensivamente estudadas, havendo sido relatada a influÃncias dessas molÃculas sobre diversos processos patolÃgicos, incluindo a carcinogÃnese. NotÃveis propriedades antitumorais tÃm sido detectadas para algumas lectinas de leguminosas, resultantes da sua habilidade em induzir a morte celular ou a autofagia em cÃlulas cancerÃgenas, o que atraÃdo atenÃÃo para suas possiveis aplicaÃÃes biomÃdicas. AlÃm disso, algumas lectinas desse grupo especificas para galactose/N-acetil-D-galactosamina (Gal/GalNAc) tÃm se mostrado Ãteis como marcadores histoquÃmicos na pesquisa do cÃncer e a caracterizaÃÃo estrutural dessas lectinas em complexo com diferentes epÃtopos cancerÃgenos vem sendo realizada com sucesso. A lectina isolada a partir das sementes da leguminosa Vatairea macrocarpa (VML) à uma lectina bem caracterizada especÃfica para Gal/GalNAc capaz de reconhecer especificamente o antÃgeno Tn (GalNAc-α-O-Ser), naturalmente encontrado em O-mucinas presentes em diferentes tipos de cÃncer. As estruturas cristalogrÃficas para a VML em complexo com o antÃgeno Tn e GalNAc foram determinadas com resoluÃÃes de 1.4 e 1.7 Ã, respectivamente. A maioria das lectinas obtidas a partir de fontes naturais consiste em misturas de diferentes isoformas, uma caracterÃstica indesejada para aplicaÃÃes biomÃdicas. Com base nisso, uma construÃÃo recombinante para VML (rVML) foi expressa em Escherichia coli, sendo obtida de forma solÃvel em com alto rendimento. A estrutura cristalina para a rVML, bem como para seus complexos com o antÃgeno Tn, GalNAc e α-Lactose foram determinadas com resoluÃÃes de 1.7, 2.7, 2 e 1.8 Ã, respectivamente, apresentando a mesma estrutura geral e padrÃes de interaÃÃo que a lectina silvestre. Com o intuito de gerar um perfil comparativo entre a VML e outras lectinas de leguminosas capazes de reconhecer o antÃgeno Tn, foram realizadas anÃlises de docking molecular utilizando fragmentos de O-mucinas diferentemente decorados com o antÃgeno Tn. Esse perfil ressalta como alteraÃÃes sutis no elenco ou disposiÃÃo dos aminoÃcidos constituintes do sÃtio de ligaÃÃo a carboidrato, que talvez nÃo influenciem a capacidade de ligaÃÃo a monossacarÃdeo, podem impactar diretamente a habilidade dessas lectinas em reconhecer antÃgenos em condiÃÃes naturais. Adicionalmente aos jà caracterizados efeitos biolÃgicos relatados para VML, a similaridade entre sua estrutura e perfis de interaÃÃes quando comparadas a outras lectinas comumente utilizadas como marcadores histoquÃmicos (e.g., VVLB4 e SBA), sugerem fortemente a possÃvel utilizaÃÃo da VML como uma nova ferramenta na pesquisa do cÃncer. Esse trabalho consiste no primeiro relato de estruturas cristalogrÃficas para uma lectina de leguminosa especÃfica para Gal/GalNAc da tribo Dalbergieae.
Lectins are a very diverse class of proteins able to bind specific sugar structures reversibly and with high specificity, but without enzymatically modifying them, triggering several important cellular processes. Among the different lectin families, legume lectins are the most thoroughly studied and have been widely reported to exhibit a number of links to many pathological processes, including carcinogenesis. The remarkable anti-tumor properties of some legume lectins, resulting from their ability to induce programmed cell death and/or autophagocytosis in cancer cells have attracted much attention for biomedical applications. Moreover, a few galactose/N-acetylgalactosamine (Gal/GalNAc)-binding lectins from this group have proven to be useful markers for cancer histochemistry, and the structural characterization of these lectins bound to specific cancer epitopes has been carried out successfully. The seed lectin isolated from the legume tree Vatairea macrocarpa (VML) is a well characterized Gal/GalNAc-binding protein able to specifically recognize naturally occurring O-mucins presenting the carcinoma epitope Tn antigen (GalNAc-α-O-Ser). The crystal structures of VML in complex with Tn antigen and GalNAc have been determined at the resolution of 1.4 and 1.7 Ã, respectively. Unfortunately, most of lectins obtained from natural sources consist in a mixture of forms, which is an undesired feature for biomedical applications. Thus, the recombinant form of VML (rVML) was expressed in Escherichia coli, being obtained soluble and wih high yielding. The crystal structure for rVML, as well as for the complex with Tn antigen, GalNAc and α-Lactose have been determined at resolutions of 1.7, 2.7, 2 and 1.8 Ã, respectively, presenting the same overall structure and binding patterns as the wild lectin. Molecular docking analysis of this new structure and other Tn-binding legume lectins to O-mucin fragments differently decorated with this antigen provides a comparative binding profile among these proteins, stressing that subtle alterations that may not influence monosaccharide binding can, nonetheless, directly impact the ability of these lectins to recognize naturally occurring antigens. In addition to the specific biological effects of VML, the structural and binding similarities between it and other lectins commonly used as histological markers (e.g., VVLB4 and SBA) strongly suggest that VML can be used as a new tool for cancer research. This is the first report of crystal structures of a Gal/GalNAc-binding legume lectin from the Dalbergieae tribe.
Howgego, Joshua David. "Synthetic lectins with novel selectivity". Thesis, University of Bristol, 2012. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.573385.
Texto completoLibros sobre el tema "Lectins"
Elumalai, Preetham y Sreeja Lakshmi, eds. Lectins. Singapore: Springer Singapore, 2021. http://dx.doi.org/10.1007/978-981-16-7462-4.
Texto completoHirabayashi, Jun, ed. Lectins. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-1292-6.
Texto completoSharon, N. y H. Lis. Lectins. Dordrecht: Springer Netherlands, 1989. http://dx.doi.org/10.1007/978-94-011-4846-7.
Texto completoSharon, Nathan y Halina Lis. Lectins. Dordrecht: Springer Netherlands, 2007. http://dx.doi.org/10.1007/978-1-4020-6953-6.
Texto completo1923-, Lis H., ed. Lectins. London: Chapman and Hall, 1989.
Buscar texto completo1923-, Lis H., ed. Lectins. 2a ed. Dordrecht: Kluwer Academic Publishers, 2003.
Buscar texto completoElumalai, Preetham, Baskaralingam Vaseeharan y Sreeja Lakshmi, eds. Aquatic Lectins. Singapore: Springer Nature Singapore, 2022. http://dx.doi.org/10.1007/978-981-19-0432-5.
Texto completoKenneth, Olden y Parent James Brian, eds. Vertebrate lectins. New York: Van Nostrand Reinhold, 1987.
Buscar texto completo1938-, Mirelman David, ed. Microbial lectins and agglutinins: Properties and biological activity. New York: Wiley, 1986.
Buscar texto completoGabius, Hans Joachim y Sigrun Gabius, eds. Lectins and Cancer. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76739-5.
Texto completoCapítulos de libros sobre el tema "Lectins"
Sharon, N. y H. Lis. "Introduction". En Lectins, 1–5. Dordrecht: Springer Netherlands, 1989. http://dx.doi.org/10.1007/978-94-011-4846-7_1.
Texto completoSharon, N. y H. Lis. "Lectin resistant cells". En Lectins, 92–96. Dordrecht: Springer Netherlands, 1989. http://dx.doi.org/10.1007/978-94-011-4846-7_10.
Texto completoSharon, N. y H. Lis. "Functions in nature". En Lectins, 97–107. Dordrecht: Springer Netherlands, 1989. http://dx.doi.org/10.1007/978-94-011-4846-7_11.
Texto completoSharon, N. y H. Lis. "Epilogue". En Lectins, 108. Dordrecht: Springer Netherlands, 1989. http://dx.doi.org/10.1007/978-94-011-4846-7_12.
Texto completoSharon, N. y H. Lis. "History". En Lectins, 6–19. Dordrecht: Springer Netherlands, 1989. http://dx.doi.org/10.1007/978-94-011-4846-7_2.
Texto completoSharon, N. y H. Lis. "Occurrence and isolation". En Lectins, 20–25. Dordrecht: Springer Netherlands, 1989. http://dx.doi.org/10.1007/978-94-011-4846-7_3.
Texto completoSharon, N. y H. Lis. "Biological activities". En Lectins, 26–36. Dordrecht: Springer Netherlands, 1989. http://dx.doi.org/10.1007/978-94-011-4846-7_4.
Texto completoSharon, N. y H. Lis. "Carbohydrate specificity". En Lectins, 37–46. Dordrecht: Springer Netherlands, 1989. http://dx.doi.org/10.1007/978-94-011-4846-7_5.
Texto completoSharon, N. y H. Lis. "Molecular properties". En Lectins, 47–58. Dordrecht: Springer Netherlands, 1989. http://dx.doi.org/10.1007/978-94-011-4846-7_6.
Texto completoSharon, N. y H. Lis. "Three dimensional structures". En Lectins, 59–64. Dordrecht: Springer Netherlands, 1989. http://dx.doi.org/10.1007/978-94-011-4846-7_7.
Texto completoActas de conferencias sobre el tema "Lectins"
Scheefers, H., A. Kobus y R. Geyer. "CARBOHYDRATE COMPOSITION AND LECTIN BINDING AFFINITIES OF HUMAN PLACENTAL TISSUE FACTOR". En XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643737.
Texto completoMurarasu, Thomas y Ludger Johannes. "Abstract 5772: Engineered lectins to treat cancer". En Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-5772.
Texto completoPetrova, N. V., O. V. Gorshkov, A. R. Nazipova y T. A. Gorshkova. "Differential expression of Nictaba lectins in flax plants". En IX Congress of society physiologists of plants of Russia "Plant physiology is the basis for creating plants of the future". Kazan University Press, 2019. http://dx.doi.org/10.26907/978-5-00130-204-9-2019-346.
Texto completoKrull, U. J., R. S. Brown, E. T. Vandenberg y B. D. Hougham. "Optical biosensors from chemical transduction by lectins and neural receptors". En Proceedings of the Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE, 1988. http://dx.doi.org/10.1109/iembs.1988.95045.
Texto completoAlen’kina, S. A. y V. E. Nikitina. "Influence of Azospirillum lectins on a stress-dependent change in the content of low-molecular antioxidants in plants". En 2nd International Scientific Conference "Plants and Microbes: the Future of Biotechnology". PLAMIC2020 Organizing committee, 2020. http://dx.doi.org/10.28983/plamic2020.019.
Texto completoO'Connell, Kathleen M., Erin E. Gatrone, Anna A. Veldkamp y John J. Lavigne. "Abstract 2013: SYNTHETIC LECTINS FOR THE DETERMINATION OF BREAST CANCER SUBTYPE". En Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-2013.
Texto completoCoêlho Bernardo, Lucas y Nathalia Regina Galvão Silva. "An alternative for healing through the use of lectins: an overview". En MOL2NET 2018, International Conference on Multidisciplinary Sciences, 4th edition. Basel, Switzerland: MDPI, 2018. http://dx.doi.org/10.3390/mol2net-04-05516.
Texto completoLakhtin, M., V. Lakhtin, S. Andina, S. Afanasiev y V. Aleshkin. "343 Complement lectin system cofunctions to other protective pro-tein systems involving relationships between lectins and glycoconjugates against autoimmune and infectious diseases". En LUPUS 2017 & ACA 2017, (12th International Congress on SLE &, 7th Asian Congress on Autoimmunity). Lupus Foundation of America, 2017. http://dx.doi.org/10.1136/lupus-2017-000215.343.
Texto completoLian, E. C. Y. y F. A. Siddigui. "BINDING OF 37-DKa PLATELET AGGLUTINATING PROTEIN TO HUMAN PLATELETS". En XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643976.
Texto completoImberty, Anne, Catherine Gautier, Julien Lescar y Ed Mitchell. "CRYSTALLOGRAPHIC AND MODELING INVESTIGATIONS OF NEW LECTINS AND THEIR COMPLEXES WITH OLIGOSACCHARIDES". En XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.383.
Texto completoInformes sobre el tema "Lectins"
Thompson, Paul R. y John J. Lavigne. Synthetic Lectins: New Tools for Detection and Management of Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, agosto de 2014. http://dx.doi.org/10.21236/ada612862.
Texto completoLavigne, John J. Synthetic Lectins: New Tools for Detection and Management of Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, agosto de 2013. http://dx.doi.org/10.21236/ada591012.
Texto completoSharon, Nathan y Maarten Chrispeels. Improvement of the Nutritional Value of Legume Storage Proteins by Genetic Engineering: Studies with Legume Lectins. United States Department of Agriculture, octubre de 1991. http://dx.doi.org/10.32747/1991.7604278.bard.
Texto completoBaliarsingh, Snigdha y Bharat Bhusan Patnaik. Identification of Novel Lectins from Freshwater Prawn, Macrobrachium rosenbergii, and Expression Analysis in Response to Vibrio harveyi and M. rosenbergii nodavirus. Peeref, julio de 2022. http://dx.doi.org/10.54985/peeref.2207p9700127.
Texto completoFluhr, Robert y Maor Bar-Peled. Novel Lectin Controls Wound-responses in Arabidopsis. United States Department of Agriculture, enero de 2012. http://dx.doi.org/10.32747/2012.7697123.bard.
Texto completoSpiegel, Yitzhak, Michael McClure, Itzhak Kahane y B. M. Zuckerman. Characterization of the Phytophagous Nematode Surface Coat to Provide New Strategies for Biocontrol. United States Department of Agriculture, noviembre de 1995. http://dx.doi.org/10.32747/1995.7613015.bard.
Texto completoKraybill, William H. Lectin Enzyme Assay Detection of Viruses, Tissue Culture, and a Mycotoxin Simulant. Fort Belvoir, VA: Defense Technical Information Center, septiembre de 1988. http://dx.doi.org/10.21236/ada276469.
Texto completoBraunschweig, Adam B., Shudan Bian y Han Xu. Carbohydrate Nanotechnology: Hierarchical Assemblies and Information Processing from Oligosaccharide-Synthetic Lectin Host-Guest. Fort Belvoir, VA: Defense Technical Information Center, septiembre de 2014. http://dx.doi.org/10.21236/ada612784.
Texto completoWang, Xin. Synthesis and Characterization of Glyconanomaterials, and Their Applications in Studying Carbohydrate-Lectin Interactions. Portland State University Library, enero de 2000. http://dx.doi.org/10.15760/etd.626.
Texto completoDeutscher, Susan. Radiolabeled Peptide Scaffolds for PET/SPECT - Optical in Vivo Imaging of Carbohydrate-Lectin Interactions. Office of Scientific and Technical Information (OSTI), septiembre de 2014. http://dx.doi.org/10.2172/1158790.
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