Abstract
A D-glucose / D-mannose specific lectin from seeds of Canavalia grandiflora (ConGF) was purified by affinity chromatography on Sephadex G-50. By SDS-PAGE ConGF yielded three protein bands with apparent molecular masses of 29-30 kDa (α chain), 16-18 kDa (β fragment) and 12-13 kDa (γ fragment), like other related lectins from the genus Canavalia (Leguminosae). ConGF strongly agglutinates rabbit erythrocytes, has a high content of ASP and SER, and its N-terminal sequence (30 residues) is highly similar to the sequences of other related lectins from subtribe Diocleinae.
Keywords: Canavalia grandiflora, (Leguminosae family), Papilionoideae, N-terminal amino acid, D-glucopyranoside, subtribe Diocleinae