PURIFICATION AND CARBOHYDRATE-BINDING SPECIFICITY OF AGROCYBE-CYLINDRACEA LECTIN

A lectin was isolated from fruiting bodies of Agrocybe cylindracea by two ion-exchange chromatographies and gel filtration on Toyopearl HW55 F. The lectin was homogeneous on polyacrylamide gel electrophoresis an d its molecular mass was determined to be 30 000 by gel filtration, an d 15 000 by sodium dodecylsulfate polyacrylamide gel electrophoresis, signifying a dimeric protein. Its carbohydrate-binding specificity was investigated both by sugar-hapten inhibition of hemagglutination and by enzyme-linked immunosorbent assay. The inhibition tests showed the affinity of the lectin to be weakly directed toward sialic acid and la ctose, and the enhanced affinity toward trisaccharides containing the NeuAc alpha 2,3Gal beta-structure. Importantly, the lectin strongly in teracted with glycoconjugates containing NeuAc alpha 2,3Gal beta 1,3Gl cNAc-/GalNAc sequences.