Isolation and characterization of novel lectins from Canavalia ensiformis DC and Dioclea grandiflora Mart. ex Benth. seeds

two lectins were isolated from canavalia ensiformis and dioclea grandiflora seeds. gel filtration produced a fraction corresponding to con a or d. grandiflora lectin while erythroagglutination assays revealed a distinct fraction presenting a lectin that agglutinates human red blood cells (rbcs) but not rabbit rbcs. hydrophobic interaction chromatography showed that the latter fraction yielded a protein that readily agglutinates human erythrocytes; the lectin was also purified by affinity chromatography on lac-sepharose showing similar properties to that of the phenyl-sepharose-purified lectin. despite minor differences (carbohydrate content or a1%1cm), the two lectins showed similar molecular properties in that they consisted of two non-covalently linked monomers having a mr of 29-30 kda and their pi values indicated that both lectins were slightly acidic proteins. the c. ensiformis lectin (cel-ii) and d. grandiflora lectin (dgl-ii) specifically recognised the h-type 2 blood group (a-l-fuc (1-2)-b-d-gal (1-4)-b-d-glcnac-o-r), while binding to h-type 1, h-type 3, h-type 4, lea or ley was weaker. carbohydrate inhibition of erythroagglutination showed that simple sugars were weakly recognised by the lectins, if at all. the n-terminal region presented a unique sequence hitherto found only in some diocleinae lectins (designated type ii). the overall results confirmed the existence of a second distinct lectin type, phylogenetically close to diocleinae species. the data indicate a functional similarity among lectins of this type which possesses distinctive characteristics differentiating them from "classical" man/glc lectins.