Hemagglutinating Activity
Mostrando 1-12 de 187 artigos, teses e dissertações.
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1. Purification, partial characterization and antimicrobial activity of Lectin from Chenopodium Quinoa seeds
Abstract A novel lectin was isolated from the seeds of Chenopodium quinoa. To achieve this end, the crude extract from the quinoa was submitted to two purification steps, Sephadex G50 and Mono Q. The hemagglutinating activity showed that this lectin agglutinates human erythrocytes. Its activity is inhibited by glucose and mannose, and remained stable under a
Food Sci. Technol. Publicado em: 24/11/2015
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2. Seeds of Amazonian Fabaceae as a source of new lectins
Seeds from fifty native Amazonian Fabaceae species (representing subfamilies Caesalpinioideae, Mimosoideae and Faboideae) were screened for the presence of new lectins. Their crude protein extracts were assayed for hemagglutinating activity (HA). The protein fractions of Anadenanthera peregrina, Dimorphandra caudata, Ormosia lignivalvis and Swartzia laevicar
Brazilian Journal of Plant Physiology. Publicado em: 2011
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3. Detecção de atividade lectínica e atividade hemolítica em extratos de esponjas (Porifera) nativas da costa atlântica do Brasil / Detection of lectinic activity and hemolytic activity in extracts of native sponges (Porifera) of atlantic coast of Brazil
Extratos aquosos de vinte espécies de esponjas da costa Atlântica brasileira foram testados para verifi cação da presença de atividade lectínica e atividade hemolítica. Hemaglutinação para eritrócitos humanos e de distintos animais foi evidenciada em 12 dos 20 extratos testados. Os extratos das espécies Axinella corrugata, Chondrilla nucula, Chond
Publicado em: 2010
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4. PurificaÃÃo, caracterizaÃÃo e determinaÃÃo de atividade coagulante da lectina de sementes de Moringa oleifera
Moringa oleifera is a tropical plant of great economic importance with several industrial and medicinal applications. Many parts of the plant are used and the seed extract is commonly employed for water purification to human consumption. Lectins are proteins or glycoproteins of nonimmune origin, which bind carbohydrates bioespecifically with agglutinant cell
Publicado em: 2009
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5. PurificaÃÃo, caracterizaÃÃo de uma lectina e compostos fenÃlicos da entrecasca de Sebastiania jacobinensis (Muill. Arg.): efeito de radiaÃÃo gama sobre estrutura-atividade protÃica e proteÃÃo de flavonÃides isolados
A lectin from Sebastiania jacobinensis bark (SejaBL) was isolated using a combination of acetone precipitation, fractionation by ammonium sulphate, ion exchange and gel filtration chromatographies. The molecular mass of SejaBL was determined as approximately 52.0kDa by SDS-PAGE and 50.0kDa by gel filtration. The lectin is a glycoprotein with a neutral carboh
Publicado em: 2009
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6. PurificaÃÃo, caracterizaÃÃo e avaliaÃÃo da atividade fÃngica da Lectina de CladÃnias de Opuntia fÃcus indica
Lectins are hemagglutinating proteins with carbohydrate binding sites; these proteins have biological properties including antimicrobial activity. The aims of this work were the isolation of Opuntia ficus indica lectin (OfÃL) and evaluation of its antifungal activity. Hemagglutinating activity (HA) of cladode crude extract (CE20%) was evaluated using rabbit
Publicado em: 2008
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7. Isolamento, caracterização termodinâmica e estudos bioquímicos da lectina de sementes dormentes e de cotilédones de sementes germinadas da leguminosa Macrotyloma axillare
The Macrotyloma axillare seed lectin (LMA) is an N-acetyl-galactosamine (GalNac) specific lectin very important in biothecnology because the specific hemmaglutination by A1 human erythrocytes. In this work, the LMA from dormant and germinated was purified by precipitation techniques and ion exchange chromatography as a new purification technique. Such method
Publicado em: 2008
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8. Atividade hemaglutinante e larvicida (Aedes aegypti) na Ãgua tratada com sementes de Moringa oleifera
Moringa oleifera seeds have been frequently used as coagulant for water treatment in Brazilian Northeast, where a high incidence of dengue fever. Lectins constitute a heterogeneous protein group capable of recognizing and reversibly binding to carbohydrates and glycoproteins. Protease inhibitors disrupt enzymatic action by formation of stable complexes with
Publicado em: 2007
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9. Análise da expressão e caracterização funcional da hemaglutinina temperatura sensível de Escherichia coli
Escherichia coli is an important agent of extra-intestinal infections both in humans and animals alike. In poultry, it is responsible for significant economic loss, being known as the pathogenic avian E. coli (APEC); and it causes colibacillosis, which starts as an infection of the respiratory tract evolving to airsacculitis, pericarditis, perihepatitis and
Publicado em: 2006
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10. PurificaÃÃo, caracterizaÃÃo e aplicaÃÃo biotecnolÃgica da(s) lectina(s) presente(s) em Bauhinia membranacea Benth
Lectins are proteins or glycoproteins of non-immune origin which bind biospecifically carbohydrates with agglutinant cell capacity of a reversible way. Plant leaves of Bauhinia genus have been used in popular medicine with properties said hypoglicemiant and diuretic. Several leaf extracts of Bauhinia membranacea Benth showed lectin presence, indicated by hem
Publicado em: 2006
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11. Levana Ferromagnetizada: uma matriz de afinidade para purificar lectina de sementes de Cratylia mollis (Cramoll 1)
Levans, fructose polymer, are composed by β-2,6 linkages and can be produced by differents species of plants and bacteria . Applications for levans have been suggested in food industries, pharmaceutics, also in medicine. Ferromagnetic particle in biomedical and industrial areas have been used. Lectins find are ubiquitously distributed in nature, and occ
Publicado em: 2006
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12. ExtraÃÃo lÃquido-lÃquido da lectina da entrecasca de Crataeva tapia l. utilizando micelas invertidas
The lectins are ubiquitous protein in the nature that reversibly bind to mono, oligo, polysaccharides and glycoconjugates. They do not present catalytic activity and unlike antibodies, are not products of immune reply. The aim of the present work was to evaluate the extraction and back-extraction of a lectin purified by ionic exchange chromatography (CrataBL
Publicado em: 2006