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dc.contributor.authorChaves, Renata Pinheiro-
dc.contributor.authorSilva, Suzete Roberta da-
dc.contributor.authorSilva, João Pedro Freire Alves da-
dc.contributor.authorCarneiro, Rômulo Farias-
dc.contributor.authorSousa, Bruno Lopes de-
dc.contributor.authorCarvalho, Fátima Cristiane Teles de-
dc.contributor.authorFarias, Wladimir Ronald Lobo-
dc.contributor.authorSousa, Oscarina Viana de-
dc.contributor.authorSilva, André Luiz Coelho-
dc.contributor.authorSampaio, Alexandre Holanda-
dc.contributor.authorNagano, Celso Shiniti-
dc.date.accessioned2023-08-03T11:48:39Z-
dc.date.available2023-08-03T11:48:39Z-
dc.date.issued2018-
dc.identifier.citationCHAVES, Renata Pinheiro; SILVA, Suzete Roberta da; SILVA, João Pedro Freire Alves da; CARNEIRO, Rômulo Farias; SOUSA, Bruno Lopes de; ABREU, Jade Oliveira; CARVALHO, Fátima Cristiane Teles de; ROCHA, Cintia Renata Costa; FARIAS, Wladimir Ronald Lobo; SOUSA, Oscarina Viana de; SILVA, André Luiz Coelho; SAMPAIO, Alexandre Holanda Sampaio; NAGANO, Celso Shiniti. Meristiella echinocarpa lectin (MEL): a new member of the OAAH-lectin family. Journal of Applied Phycology , Germany, v. 128, p. 87-92, 2018. Disponível em: https://doi.org/10.1007/s10811-018-1473-7. Acesso em:03 ago 2023.pt_BR
dc.identifier.uri0177-5103-
dc.identifier.urihttp://www.repositorio.ufc.br/handle/riufc/73814-
dc.description.abstractA new lectin from the marine red alga Meristiella echinocarpa (MEL) was isolated and biochemically characterized. MEL is a monomeric protein of 28 kDa with specificity for yeast mannan. Hemagglutination activity of MEL was stable between pH 5 and 10, temperatures up to 50 °C, and neither EDTA nor divalent ions affected it. The complete amino acid sequence of MEL was determined through a combination of tandem mass spectrometry and DNA cloning. As a new member of the OAAH-lectin family, the primary structure of MEL consists of 267 amino acid residues distributed in four tandem repeat domains, sharing at least 48% of identity. Theoretical secondary structure of MEL was composed of 3% α-helix, 40% β-sheet, 19% β-turn, and 38% coil. Melting temperatures of the lectin in the absence and presence of mannan were 54 and 61 °C, respectively. Furthermore, MEL was able to recognize and agglutinate pathogenic bacterial strains, such as multidrug-resistant Salmonella and Vibrio alginolyticus. Keywords . . OAAH-family . Pathogenic bacteriapt_BR
dc.language.isoenpt_BR
dc.publisherJournal of Applied Phycologypt_BR
dc.subjectLectinpt_BR
dc.subjectSpecies - Rhodophytapt_BR
dc.subjectPathogenic bacteriapt_BR
dc.subjectLecitinapt_BR
dc.subjectEspécie - Rhodophytapt_BR
dc.subjectBactérias patogênicaspt_BR
dc.titleMeristiella echinocarpa lectin (MEL): a new member of the OAAH-lectin familypt_BR
dc.typeArtigo de Periódicopt_BR
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