Studies on Ricinus communis lectin--carbohydrate interaction by means of affinity electrophoresis.
The affinity gel electrophoresis of lectins purified from the seeds of Ricinus communis was studied. The mobilities of lectins on the gel showed various degree of retardation with their affinity toward their macromolecular ligand-agarose. Ricinus agglutinin which possessed the strongest affinity was retarded strongly, ricin C, and ricin B moderately, and ricin A, weakly. The concentrations of free moving ligand-galactose to reduce the retardation were also correlated very well with the potencies of affinities of lectins toward the ligand. The Kd values calculated from the retardations were 4.32 microM, 18.32 microM, 28.13 microM and 52.88 microM for ricinus agglutinin, ricin C, ricin B and ricin A respectively. Affinity gel electrophoresis was found to be a simple and quick method for studying the interaction of lectins with their ligands.
D002241:Carbohydrates; D002367:Ricinus communis; D002846:Chromatography, Affinity / Q000379:methods; D002850:Chromatography, Gel / Q000379:methods; D004589:Electrophoresis, Disc / Q000379:methods; D005690:Galactose; D037102:Lectins / Q000302:isolation & purification*; D037121:Plant Lectins; D010947:Plants, Toxic; D012278:Ricinus
D002241:Carbohydrates; D037102:Lectins; D037121:Plant Lectins; C017707:Ricinus communis agglutinin-1; D005690:Galactose