CaracterizaÃÃo da lectina de Eugenia malaccensis l. (emal): avaliaÃÃo de atividades biolÃgicas

AUTOR(ES)

Vanessa Passos Brustein

DATA DE PUBLICAÇÃO

2006

RESUMO

using ammonium sulphate fractionation (F0-80), followed by affinity chromatography in Sephadex G-50 column. Hemmaglutinating activity (HA) was evaluated in presence of ions (Ca2+ and Mg2+), carbohydrates, glycoproteins, or after treatment with different temperatures and pH values (2 â 12). Antimicrobial activity of EmaL was investigated by the disc diffusion method against Gram-positive and Gramnegative bacteria. Chromatography in Sephadex G-50 column showed a protein peak biospecific eluted using glucose, exhibiting three protein peaks whith molecular masses of 112, 28 and 14 kDa by gel filtration using a ÃKTAFPLC system. The purified lectin showed a main protein band in SDS-PAGE (14 kDa). EmaL HA is totally inhibited by glucose, casein, ovoalbumine and fetuin, is not dependent of ions, is dependent of pH and is totally reduced by heating at 30 ÂC. EmaL inhibited growth of tested microorganisms; best result (26.5 mm  1.2 halo) was obtained with Staphylococcus aureus, with minimal inhibitory concentration (MIC) of 1.5 μg/ml and minimal bactericide concentration (MBC) of 15 μg/ml. In conclusion, EmaL is a powerful antimicrobial agent of low cost with wide spectrum of action

ASSUNTO(S)

glicoproteÃnas lectina eugenia malaccensis bioquimica

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