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Characterization of proteins phosphorylated by the cAMP‐dependent protein kinase of bovine heart mitochondria

1995; Wiley; Volume: 377; Issue: 3 Linguagem: Inglês

10.1016/0014-5793(95)01407-1

1873-3468

Anna Maria Sardanelli, Zuzana Technikova-Dobrova, Salvatore Scacco, Francesco Speranza, Sergio Papa,

Protein Structure and Dynamics

Characterization of two mitochondrial proteins of M 1 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, III 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.