Abstract
The mechanism of action of ricin, an irreversible inhibitor of protein synthesis in eukaryotic ribosomes, has been studied with ethanol extracted 80S rat liver ribosomes. The results show that the irreversible action of the toxin is on a component of the ribosome which remains in the core ribosome after the removal of the ethanol soluble proteins. The acid phosphoproteins P1 and P2 are shown not to be the site of action of the toxin.
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