Rabbit reticulocyte ribosomes were incubated with polyuridylic acid at 37° for 1 h under conditions suitable for protein synthesis. Ribosomes containing bound polyuridylic acid were isolated and dissociated into subparticles by treatment with EDTA. The subparticles were separated by zone centrifugation in a sucrose density gradient and the distribution of polyuridylic acid was examined by measuring the ability of gradient fractions to stimulate the incorporation of [14C] phenylalanine into protein by a cell‐free system. It was observed that the peak of polyuridylic acid activity corresponded to a region of the subparticle gradient having a sedimentation coefficient of about 50 S. When [14C] polyuridylic acid was used in the initial binding reaction, subsequent analysis of subparticles produced by treatment with EDTA confirmed the presence of polyuridylic acid on or close to the large ribosomal subparticle. Copyright © 1969, Wiley Blackwell. All rights reserved