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Pisum sativum agglutinin is nearly identical in structure and carbohydrate specificity to Lens culinaris agglutinin. PSA has four subunits, two of approximately 17,000 daltons and two of about 6,000 daltons. Isoelectric focusing has revealed two isolectins with isoelectric points of pH 5.9 and pH 7.0. The lectin has specificity toward a-linked mannose-containing oligosaccharides, with an N-acetylchitobiose-linked a-fucose residue included in the receptor sequence. Calcium and manganese ions are required for activity. PSA has been used to fractionate cells, to isolate glycoproteins and glycopeptides, to distinguish between normal and virally transformed cells, as a T-cell mitogen, and as an inhibitor of allograft rejection.
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. |