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, 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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphatases / metabolism
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Adenosine Triphosphate / metabolism
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Animals
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Carrier Proteins*
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Cattle
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Cyclic AMP-Dependent Protein Kinases / metabolism*
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Electron Transport Complex IV / metabolism
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Electrophoresis, Gel, Two-Dimensional
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Membrane Proteins / metabolism
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Mitochondria, Heart / enzymology
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Mitochondria, Heart / metabolism*
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Mitochondrial Proton-Translocating ATPases
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NAD(P)H Dehydrogenase (Quinone) / metabolism
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Phosphoproteins / biosynthesis*
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Phosphorylation
Substances
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Carrier Proteins
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Membrane Proteins
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Phosphoproteins
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Adenosine Triphosphate
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NAD(P)H Dehydrogenase (Quinone)
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Electron Transport Complex IV
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Cyclic AMP-Dependent Protein Kinases
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Adenosine Triphosphatases
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Mitochondrial Proton-Translocating ATPases
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oligomycin sensitivity-conferring protein