Macromolecular properties of Diocleinae lectins

Structural properties of six closely related lectins isolated from plants belonging from the legume group Diocleinae were studied in solution. Affinity and gel filtration chromatography of the lectins at different pH conditions demonstrated that the lectins diverge in affinity for a specific matrix mainly at the pH range 4.0 up to 6.0 and that at neutral pH they tend to form dimers. Analysis of circular dichroism and fluorescence emission spectra stressed the differences of the lectin from Cratylia floribunda seeds from that of Canavalia brasiliensis, C. ensisformis, C. maritima, Diolcea grandiflora and D. virgata. According to the results, these proteins constitute a excellent model to study fine protein structure/function relationships.