Although the specificity of this lectin is not well defined, MAL II appears to bind only particular carbohydrate structures that contain sialic acid. Unlike SNA which seems to prefer structures with (a-2,6) linked sialic acid, MAL II appears to bind sialic acid in an (a-2,3) linkage. While fetuin is a poor inhibitor, glycophorin is a very potent inhibitor of MAL II binding. Tissue staining patterns are also very different among MAL I, SNA and MAL II. This biotinylated lectin conjugate is prepared from affinity-purified lectin and is optimally labeled with biotin. Essentially free of inactive lectin conjugate and containing no free biotin, this biotinylated lectin provides an ideal intermediate for examining glycoconjugates using the Biotin-Avidin System. First the biotin-labeled lectin is added, followed by the VECTASTAIN® ABC Reagent, Avidin D conjugate, or streptavidin derivative. Another possible application is in the isolation of lymphokines and other products of mitogenic stimulation. |