Abstract
Incorporation of radioactive phosphate into hot HClO4 residue derived from synaptosomal particulate and soluble fractions was studied using a double-isotope technique. Increased phosphorylation was observed only in the particulate fractions of foot-shock avoidance-conditioned mice compared with quiet controls. Similar results were obtained irrespective of whether discontinuous sucrose or Ficoll—sucrose gradients were used to isolate the synaptosome-enriched fractions. Enzymatic and chemical characterization showed the radioactive label in the hot HClO4 residue to be due to phosphorus covalently bound to proteins.
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