Abstract
Young rats were fed high or low phenylalanine diets for periods up to 40 days. The free and membrane-bound ribosomes were isolated and their proteins were extracted and analyzed by means of the two-dimensional polyacrylamide gel electrophoresis. No qualitative differences were found in the proteins extracted from either the free or the membrane-bound ribosomes of rats fed the high phenylalanine diet as compared with control animals. On the other hand, proteins extracted from both classes of ribosomes isolated from rats kept on low phenylalanine diet were found to be deficient in one protein. Examination of the protein patterns of the large and small subunits revealed that the missing protein is a large subunit protein. However, complete starvation of young rats for one week gave ribosomal protein patterns which when compared to those of normal rats were found to be deficient in a small subunit protein. These missing proteins cannot be removed from normal liver monosomes by KCl washing and can be considered as real ribosomal proteins.
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