The affinity of rat liver ribosome subunits for degranulated rough microsomal membranes.
Potassium and magnesium ion concentrations affected the extent but not the specificity of binding in vitro of 60-S and 40-S ribosome subunits to degranulated rough microsomal membranes from rat liver. Scatchard plots revealed that under ionic conditions most likely to resemble those in vivo, the affinity constants for binding 60-S subunits were approximately four-times greater than those characterizing 40-S subunit binding. Further, the extent to which subunits bound at saturation was close to the level of ribosomes present in intact membranes.
D000818:Animals; D001665:Binding Sites; D007700:Kinetics; D008099:Liver / Q000648:ultrastructure*; D008274:Magnesium / Q000494:pharmacology; D008566:Membranes / Q000187:drug effects / Q000648:ultrastructure*; D008862:Microsomes, Liver / Q000187:drug effects / Q000648:ultrastructure*; D009994:Osmolar Concentration; D011188:Potassium / Q000494:pharmacology; D051381:Rats; D012270:Ribosomes / Q000187:drug effects / Q000648:ultrastructure*
D008274:Magnesium; D011188:Potassium