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Phosphorylation of mitochondrial proteins in bovine heart
Author(s) -
Technikova-Dobrova Zuzana,
Sardanelli Anna Maria,
Papa Sergio
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81109-d
Subject(s) - mitochondrion , phosphorylation , protein kinase a , biochemistry , protein phosphorylation , chemistry , atp–adp translocase , microbiology and biotechnology , biology , inner mitochondrial membrane
Protein phosphorylation by [γ‐ 32 P]ATP in total extract and subfractions of bovine heart mitochondria has been studied. The results show that, in addition to pyruvate dehydrogenase, three mitochondrial proteins, with molecular weights of 44,000, 39,000 and 31,000 Da, are phosphorylated by a cAMP‐independent mitochondrial protein kinase. Three other proteins associated with mitochondria, with molecular weights of 125,000, 19,000 and 6,500 Da, are phosphorylated by the cytoplasmic cAMP‐dependent protein kinase (kinase A).