Purification and physicochemical properties of ricins and agglutinins from Ricinus communis.
Two toxin ricins and two agglutinins have been purified from the seeds of Ricinus communis by an improved procedure based on ion-exchange chromatography and gel filtration. One of the two purified ricins binds to Sepharose 4B while the other does not. The physicochemical properties of the four Ricinus lectins are presented and the possible relationships of these Ricinus lectins to those previously described are discussed.
D000596:Amino Acids / Q000032:analysis; D002847:Chromatography, Agarose; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003208:Concanavalin A / Q000276:immunology; D004591:Electrophoresis, Polyacrylamide Gel; D005779:Immunodiffusion; D037102:Lectins / Q000302:isolation & purification*; D008970:Molecular Weight; D037121:Plant Lectins; D010940:Plant Proteins / Q000302:isolation & purification*; D010947:Plants, Toxic; D012276:Ricin / Q000302:isolation & purification*; D012278:Ricinus / Q000032:analysis*; D012967:Sodium Dodecyl Sulfate
D000596:Amino Acids; D037102:Lectins; D037121:Plant Lectins; D010940:Plant Proteins; C017707:Ricinus communis agglutinin-1; D003208:Concanavalin A; D012967:Sodium Dodecyl Sulfate; D012276:Ricin