Abstract
In vitro phosphorylation of ribosomal proteins by a ribosomal protein kinase has revealed that the initial rate and the final level of phosphorylation vary with conditions under which the cells are cultivated. Cells grown in medium containing serum yield the most active ribosomes, while those maintained in protein-free medium are least active. Cells exposed to insulin as the sole protein produce ribosomes intermediate in phosphorylating activity. The shift in phosphorylating activity occurs within 2 hours after the modification of the growth conditions. The protein kinase and the substrate proteins can be resolved by a difference in heat stability, by detergent and high salt elution and by column fractionation.
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