Poly(A)-containing mRNA has been prepared from the polyribosomes and post-polyribosomal mRNP fraction of duck reticulocytes. The coding capacity of the respective mRNA populations has been examined by translation in vitro followed by two-dimensional electrophoresis of the 35S-labeled polypeptides. A detailed analysis of these results is given elsewhere (Imaizumi-Scherrer, M.-T., Maundrell, K., Civelli, O., and Scherrer, K. (1982) Dev. Biol. 93, 126-138). Here, we focus on one of these translation products which migrates as a slightly basic protein of 73,000 molecular weight. By two-dimensional electrophoretic analysis and partial peptide mapping, we show that this protein is indistinguishable from the poly(A)-binding protein. We conclude that the majority of the coding sequences for this protein are translationally repressed in the reticulocyte cytoplasm.