Characterization of two mitochondrial proteins of M(r) 42 and 18 kDa, respectively, phosphorylated by the cAMP-dependent protein kinase of bovine heart mitochondria (mtPKA), is presented, A 42 kDa protein is found to be loosely associated to complexes I, UI and IV of the respiratory chain and complex V (ATP synthase) in the inner mitochondrial membrane, An 18 kDa protein is associated to complex I in the inner membrane and in a purified preparation of this complex where it can be phosphorylated by the isolated catalytic subunit of PKA.
Characterization of proteins phosphorylated by the cAMP-dependent protein kinase of bovine heart mitochondria
SARDANELLI, Anna Maria;SCACCO, Salvatore;
1995-01-01
Abstract
Characterization of two mitochondrial proteins of M(r) 42 and 18 kDa, respectively, phosphorylated by the cAMP-dependent protein kinase of bovine heart mitochondria (mtPKA), is presented, A 42 kDa protein is found to be loosely associated to complexes I, UI and IV of the respiratory chain and complex V (ATP synthase) in the inner mitochondrial membrane, An 18 kDa protein is associated to complex I in the inner membrane and in a purified preparation of this complex where it can be phosphorylated by the isolated catalytic subunit of PKA.File in questo prodotto:
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