| Autor: |
Chaves, Renata Pinheiro, da Silva, Suzete Roberta, da Silva, João Pedro Freire Alves, Carneiro, Rômulo Farias, de Sousa, Bruno Lopes, Abreu, Jade Oliveira, de Carvalho, Fátima Cristiane Teles, Rocha, Cintia Renata Costa, Farias, Wladimir Ronald Lobo, de Sousa, Oscarina Viana, Silva, André Luiz Coelho, Sampaio, Alexandre Holanda, Nagano, Celso Shiniti |
| Zdroj: |
Journal of Applied Phycology; Aug2018, Vol. 30 Issue 4, p2629-2638, 10p |
| Abstrakt: |
A 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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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