[Characteristics of the biosynthesis and phosphorylation of cytoplasmic proteins from different parts of brain and liver of rats under functional influences].

The biosynthesis and phosphorylation of peptide fractions from rat liver cytoplasm and from different divisions of rat brain differing in their electrophoretic mobilities during polyacrylamide gel electrophoresis with Na-DS were studied under normal conditions and at intensive locomotor exercise. In brain trunk the incorporation of [14C]methionine into nearly all peptide fractions and the phosphorylation were found to be considerably decreased. In neocortical preparations the changes in biosynthesis were different depending on the nature of protein fractions, which can partly be due to the oppositely directed types of [14C]methionine incorporation into the neurons and glyal cells, i. e. decrease and considerable increase, respectively. The level of phosphorylation of neuronal proteins was significantly decreased in the cytoplasm and considerably increased in the glyal cells. The rate of biosynthesis in all the peptide fractions and the phosphorylation were considerably increased in cerebellar preparations, which was not the case in other brain divisions and in the liver.