Abstract
After treatment of chick lens polysomes with EDTA, two ribonucleoprotein components sedimenting between the smaller ribosomal subunit and transfer RNA can be isolated on sucrose density gradients. The RNA from the larger ribonucleoprotein component sediments at approximately 15S and that from the smaller at approximately 9S, but in both cases the RNA is heterodisperse. When the pooled putative lens mRNA is added to a duck reticulocyte or mouse Landschutz ascites cell lysate system, the synthesis of chick lens crystallins is stimulated, as judged by specific immunological criteria and gel electrophoresis.
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