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Galanthus nivalis lectin is a small molecular weight tetramer consisting of subunits of about 13,000 daltons. It has an isoelectric point below pH 4.6. The lectin contains little or no carbohydrate and, unlike most mannose-specific lectins, is not a metalloprotein and does not require Ca++ or Mn++ for binding.
Binding seems to be preferentially directed toward structures containing (a-1,3) mannose residues. Also in contrast to most mannose-binding lectins, GNL will not bind alpha linked glucose. Reports indicate that this lectin binds IgM but not IgG of the immunoglobulin classes of rat and mouse. The only protein from human serum reported to bind to this lectin is a2-macroglobulin.
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. |