%0 Journal Article
%T Isolation and characterization of novel lectins from Canavalia ensiformis DC and Dioclea grandiflora Mart. ex Benth. seeds
%A Melgarejo
%A Luz Marina
%A Vega
%A Nohora
%A P¨Śrez
%A Gerardo
%J Brazilian Journal of Plant Physiology
%D 2005
%I Scientific Electronic Library Online
%R 10.1590/S1677-04202005000300006
%X 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.
%K diocleinae
%K leguminoseae
%K characterization
%K lectins.
%U http://www.scielo.br/scielo.php?script=sci_abstract&pid=S1677-04202005000300006&lng=en&nrm=iso&tlng=en