[cAMP-dependent phosphorylation in the pig brain].
Protein phosphorylation in the cytosol, membranes and nuclei of pig brain cells was investigated. Endogenous cAMP-dependent phosphorylation was observed in all fractions studied. The degree of activation of this process by cAMP was different, depending on the fraction. The molecular weights of the endogenous protein substrates were found to be equal to 60 000, 45 000 and 28 000 for the nuclei, 80 000, 71 000, 31 000, 25 000, 16 000 and 11 000 for the membranes and 280 000, 80 000, 67 000, 53 000, 32 000, 25 000 and 22 000 for cytosol. It was shown that the majority of these proteins can be phosphorylated by the exogenous cAMP-dependent pig brain protein kinase.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002467:Cell Nucleus / Q000201:enzymology; D000242:Cyclic AMP / Q000378:metabolism*; D003600:Cytosol / Q000201:enzymology; D007700:Kinetics; D008970:Molecular Weight; D010766:Phosphorylation; D010770:Phosphotransferases / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism; D013552:Swine
D000242:Cyclic AMP; D010770:Phosphotransferases; D011494:Protein Kinases
cAMP-zavisimoe fosforilirovanie belkov mozga svin'i.