Abstract
We have previously shown [ 1 ] that some ribosomal proteins of rat liver were phosphorylated in vivo, on serine residues and that isolated ribosomes of rat liver could also be phosphorylated in vitro by ATP and a kinase from microsomal supernatant of rat liver. This phosphorylation was estimated by cyclic AMP at physiological doses (half-stimulation at 5 X 1 O-' M). It is well known that cyclic AMP is the cellular mediator of glucagon in rat liver [2] . Therefore we have studied the effects of glucagon on the in vivo phosphorylation of ribosomal proteins of rat liver. We have observed that 30 min after injection of glucagon and H, 32P0,, phosphorylation of ribosomal proteins was strongly increased. Autoradiography after electrophoresis of these proteins showed that phosphorylation of one of these proteins was stimulated 2 or 3 fold after injection of glucagon.
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