PHOSPHORYLATION OF MITOCHONDRIAL PROTEINS IN BOVINE HEART - CHARACTERIZATION OF KINASES AND SUBSTRATES

Authors
TECHNIKOVADOBROVA Z SARDANELLI AM PAPA S
Citation
Z. Technikovadobrova et al., PHOSPHORYLATION OF MITOCHONDRIAL PROTEINS IN BOVINE HEART - CHARACTERIZATION OF KINASES AND SUBSTRATES, FEBS letters, 322(1), 1993, pp. 51-55
Citations number
18
Categorie Soggetti
Biophysics,Biology
Journal title
FEBS letters → ACNP
ISSN journal
00145793
Volume
322
Issue
1
Year of publication
1993
Pages
51 - 55
Database
ISI
SICI code
0014-5793(1993)322:1<51:POMPIB>2.0.ZU;2-2
Abstract
Protein phosphorylation by [gamma-P-32]ATP in total extract and subfra ctions of bovine heart mitochondria has been studied. The results show that, in addition to pyruvate dehydrogenase, three mitochondrial prot eins, with molecular weights of 44,000, 39,000 and 31,000 Da, are phos phorylated by a cAMP-independent mitochondrial protein kinase. Three o ther proteins associated with mitochondria, with molecular weights of 125,000, 19,000 and 6,500 Da, are phosphorylated by the cytoplasmic cA MP-dependent protein kinase (kinase A).