cAMP-dependent protein kinases of rat pituitary GH3 cells.
Two isoenzymes (type I and type II) of cAMP-dependent protein kinases were found in GH3 cytosol, isozyme type II activity being the predominant form (approximately 90%). Photoaffinity labeling of GH3 cell extracts with 8-N3-[32P]cAMP revealed three cAMP-binding proteins exhibiting molecular weights of 53,000, 51,000 and 48,000, respectively. The latter represents the regulatory subunit of type I isoenzyme whereas the 53,000 and 51,000 cAMP-binding proteins correspond to two different molecular forms of the type II isoenzyme regulatory subunit which are phosphorylated by a cAMP-dependent mechanism.
Fabbro
D
D
Bally
K
K
Koudelka
G
G
Jungmann
R A
RA
Eppenberger
U
U
D000818:Animals; D002478:Cells, Cultured; D000242:Cyclic AMP / Q000378:metabolism; D003600:Cytosol / Q000201:enzymology; D007527:Isoenzymes / Q000032:analysis*; D008970:Molecular Weight; D010766:Phosphorylation; D010902:Pituitary Gland / Q000201:enzymology*; D011485:Protein Binding; D011494:Protein Kinases / Q000032:analysis*; D011506:Proteins / Q000378:metabolism; D051381:Rats
D007527:Isoenzymes; D011506:Proteins; D000242:Cyclic AMP; D011494:Protein Kinases