Abstract
Chemical evidence is provided that glycogen synthase extracted from rabbit liver, heart, kidney and brain and from frog liver and muscle all are phosphorylated by [ 32P]ATP in the presence of protein kinase. After partial acid hydrolysis, serine phosphate together with a number of labeled peptides were observed. The peptide maps were similar and allowed a provisional differentiation of the phosphorylated sites into four separate sites including (a) frog liver, (b) frog muscle, (c) rabbit skeletal muscle, and (d) rabbit heart, brain, kidney and liver. The major labelled chymotryptic peptides of glycogen synthase and phosphorylase were compared and found to differ markedly in their electrophoretic behavior. On partial rehydrolysis of these chymotryptic peptides with acid, identical phosphopeptide maps were obtained. This proves that within the larger non-identical chymotryptic peptides there is present the identical hexapeptide sequences previously established.
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