Willian F Reis, Marcos E S Silva, Ana C S Gondim, Renato C F Torres, Rômulo F Carneiro, Celso S Nagano, Alexandre H Sampaio, Claudener S Teixeira, Lenita C B F Gomes, Bruno L Sousa, Alexandre L Andrade, Edson H Teixeira, Mayron A Vasconcelos
In this study, we purified a lectin isolated from the seeds of Dioclea bicolor (DBL) via affinity purification. Electrophoresis analysis revealed that DBL had three bands, α, β, and γ chains, with molecular masses of approximately 29, 14, and 12 kDa, respectively. Gel filtration chromatography revealed that the native form of DBL had a molecular mass of approximately 100 kDa, indicating that it is a tetramer. Interestingly, DBL-induced hemagglutination was inhibited by several glucosides, mannosides, ampicillin, and tetracycline with minimum inhibitory concentration (MIC) values of 1...
April 14, 2024: Protein Journal