Purification and lectins from Ricinus communis by combination of affinity and ion-exchange chromatography and characterization of the isolated proteins.
Lectins in the seeds of Ricinus communis L. were separated by affinity chromatography using stromata, and 3 fractions obtained by ion-exchange chromatography. Polyacrylamide-gel electrophoresis showed that 2 fractions were homogeneous and that 1 fraction gave 2 bands. Immunoelectrophoresis with rabbit antisera and polyacrylamide-gel isoelectric focusing showed that the 3 fractions were separate and distinct entities consisting of many proteins with isoelectric points near the isoelectric point of the main protein. The molecular weights of the separated proteins and their subunits were studied by SDS polyacrylamide-gel electrophoresis.
D000818:Animals; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D006386:Hemagglutination Tests; D007525:Isoelectric Focusing; D037102:Lectins / Q000302:isolation & purification*; D008970:Molecular Weight; D010455:Peptides; D037121:Plant Lectins; D010940:Plant Proteins; D010947:Plants, Toxic; D011817:Rabbits; D012278:Ricinus
D037102:Lectins; D010455:Peptides; D037121:Plant Lectins; D010940:Plant Proteins