Eukaryote ribosomes possess a binding site for concanavalin A.
Ribosomes prepared from chicken liver or rabbit reticulocytes bound concanavalin A in a molar ratio of approximately 1:1. This binding is to the large subunit of the eukaryote ribosomes with a dissociation constant of 5 X 10(-7) M (0 degrees). The binding of concanavalin A to Escherichia coli ribosomes was much less. Binding to the RNA or to possible membrane contaminants was ruled out in control experiments. Chicken liver ribosomes were labeled in vivo with 3H-labeled amino acids, purified, and dissociated in sodium dodecyl sulfate. Affinity chromatography of this preparation made it possible to isolate the small proportion of the ribosomal proteins (about 1.5%) containing the concanavalin A binding site. This protein moved as a single band during electrophoresis on polyacrylamide gels containing sodium dodecyl sulfate and showed an apparent molecular weight of 31,000.
D000818:Animals; D001665:Binding Sites; D002645:Chickens; D003208:Concanavalin A / Q000378:metabolism*; D004926:Escherichia coli; D007700:Kinetics; D008566:Membranes / Q000378:metabolism; D008970:Molecular Weight; D012335:RNA, Ribosomal / Q000378:metabolism; D011817:Rabbits; D012269:Ribosomal Proteins / Q000302:isolation & purification / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism* / Q000648:ultrastructure; D013045:Species Specificity
D012335:RNA, Ribosomal; D012269:Ribosomal Proteins; D003208:Concanavalin A