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- W2479453440 abstract "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 (00). The binding of concanavalin A to Escherichia coli ri- bosomes 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 H-labeled amino acids, purified, and dissociated in sodium dodecyl sul- fate. Affinity chromatography of this preparation made it pos- sible 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." @default.
- W2479453440 created "2016-08-23" @default.
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- W2479453440 date "2016-01-01" @default.
- W2479453440 modified "2023-09-27" @default.
- W2479453440 title "Eukaryote ribosomes possess a binding site for concanavalin A (affinity chromatography/chicken liver/Con A binding/Escherichia coli/rabbit reticulocytes)" @default.
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