| Popis: |
Using the polyacrylamide gel electrophoresis (PAGE) of the synaptic membranes of proteins isolated from the rat brain cortex it is shown that on phosphorylation in the presence of [gamma-33P] GTP (5 and 10 microM) and 10-20-fold excess of unlabelled ATP the phosphorylation of protein with molecular weights of 41,000 and 49,000 Dalton greatly increased but the labelling of proteins with molecular weights of 54000 and 30,000 Dalton strongly decreased or was completely abolished. The addition of unlabelled ATP practically does not change the phosphorylation of the bands (proteins) with molecular weights of 86,000, 82,000, 46,000 Dalton and weakly decreased when labelling proteins with molecular weight of 59,000. The results obtained permit suggesting the existence of proteins--substrates of specific phosphorylation with GTP in synaptic membranes. |
