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JBC, Vol. 251, Issue 23, 7526-7529, Dec, 1976
R. Rangel-Aldao and O. M. Rosen
The adenosine 3':5'-monophosphate (cAMP)-dependent protein kinase purified
from bovine cardiac muscle catalyzes the transfer of up to 2 mol of 32P
from [lambda-32P]ATP to seryl residues in its cyclic nucleotide-binding
protein component (Erlichman, J., Rosenfeld, R., and Rosen, O. M. (1974) J.
Biol. Chem. 249, 5000-5003). We now present three lines of evidence to
support our conclusions that the undissociated holoenzyme does not catalyze
the phosphorylation of exogenous substrates but can undergo
self-phosphorylation by an intramolecular reaction: (a) addition of either
cAMP-binding protein or the protein kinase inhibitor (Walsh, D. A., Ashby
C. D., Gonzales, C., Calkins, D., Fischer, E. H., and Krebs, D. G. (1971)
J. Biol. Chem. 241, 1977-1985) does not inhibit self-phosphorylation as it
does phosphorylation of exogenous substrates in the presence or absence of
cAMP; (b) addition of catalytic subunit to an excess of cyclic
nucleotide-binding protein results in phosphorylation equivalent to the
amount of holoenzyme so generated; (c) the rate of self-phosphorylation is
not affected by dilution of the holoenzyme.
Mechanism of self-phosphorylation of adenosine 3':5'-monophosphate-dependent protein kinase from bovine cardiac muscle
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