Study of autophosphorylation of isoenzymes of cyclic AMP-dependent protein kinases.
Type I and type II cyclic AMP-dependent protein kinases, present in the cytosol from each of five rat and two bovine tissues, were separated from one another by DEAE-cellulose column chromatography in order to study their possible autophosphorylation. In each of the tissues studied, autophosphorylation of the regulatory subunit of the cyclic AMP-dependent protein kinase by the catalytic subunit could be demonstrated with the type II enzyme but not with the type I enzyme.
D000818:Animals; D001921:Brain / Q000201:enzymology; D002417:Cattle; D000242:Cyclic AMP / Q000494:pharmacology; D003600:Cytosol / Q000201:enzymology; D005260:Female; D007527:Isoenzymes / Q000378:metabolism; D008099:Liver / Q000201:enzymology; D009206:Myocardium / Q000201:enzymology; D010750:Phosphoproteins / Q000096:biosynthesis*; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats; D014599:Uterus / Q000201:enzymology
D007527:Isoenzymes; D010750:Phosphoproteins; D000242:Cyclic AMP; D011494:Protein Kinases