[Study of the endogenous cyclic nucleotide-dependent phosphorylation of synaptic membrane proteins].
The highest activity of cyclic nucleotide-dependent (cAMP--2 X 10(-5) M, GMP--2 X 10(-4) M) phosphorylation of synaptic membrane proteins in vitro is revealed at equimolar concentrations of ATP and Mg2+ (10(-3)M) and depends on the ratio of the ATP concentration, protein amount in the assay and the period of exposure. At concentrations exceeding 10(-3) M ATP inhibits cyclic nucleotide-dependent phosphorylation. Optimal concentrations of ATR and Mg2+ to provide basal phosphorylation are found to be equal to 10(-2) M. Possible role of cyclic nucleotide-dependent phosphorylation in synaptic transmission is discussed.
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D007700:Kinetics; D008274:Magnesium; D008565:Membrane Proteins / Q000378:metabolism*; D010766:Phosphorylation; D051381:Rats; D011919:Rats, Inbred Strains; D013570:Synaptic Membranes / Q000378:metabolism*
D008565:Membrane Proteins; D000255:Adenosine Triphosphate; D008274:Magnesium
Issledovanie éndogennogo tsiklonukleotidzavisimogo fosforilirovaniia belkov sinapticheskikh membran.