cAMP-dependent protein phosphorylation in mitochondria of bovine heart.
A study is presented of the cAMP-dependent phosphorylation in bovine heart mitochondria of three proteins of 42, 16 and 6.5 kDa associated to the inner membrane. These proteins are also phosphorylated by the cytosolic cAMP-dependent protein kinase and by the purified catalytic subunit of this enzyme. In the cytosol, proteins of 16 and 6.5 kDa are phosphorylated by the cAMP-dependent kinase. It is possible that cytosolic and mitochondrial cAMP-dependent kinases phosphorylate the same proteins in the two compartments.
Technikova-Dobrova
Z
Z
Institute of Medical Biochemistry and Chemistry, University of Bari, Italy.
Sardanelli
A M
AM
Stanca
M R
MR
Papa
S
S
D000818:Animals; D002417:Cattle; D000242:Cyclic AMP / Q000502:physiology*; D017868:Cyclic AMP-Dependent Protein Kinases / Q000378:metabolism*; D003600:Cytosol / Q000378:metabolism; D008929:Mitochondria, Heart / Q000378:metabolism*; D008970:Molecular Weight; D010750:Phosphoproteins / Q000737:chemistry / Q000378:metabolism*; D010766:Phosphorylation
D010750:Phosphoproteins; D000242:Cyclic AMP; D017868:Cyclic AMP-Dependent Protein Kinases