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J. Biol. Chem., Vol. 262, Issue 8, 3534-3540, 03, 1987
SO Doskeland, OK Vintermyr, JD Corbin and D Ogreid
The rate and equilibrium kinetics of [3H]cGMP binding to the two rapidly
exchanging and two slowly exchanging sites of dimeric cGMP- dependent
protein kinase from bovine lung were studied. As observed by McCune and
Gill (McCune, R. W., and Gill, G. N. (1979) J. Biol. Chem. 254, 5083-5091),
unlabeled cGMP retarded the dissociation of [3H]cGMP bound to the "slow"
site. This effect was due to interaction of unlabeled cGMP with the "rapid"
rather than the slow site. First, the potencies of unlabeled cGMP and a
number of cGMP analogs correlated nearly perfectly with their affinities
for the rapid site. Second, the rate of dissociation in the absence of
unlabeled ligand was independent of the degree of saturation of the slow
sites. Third, unlabeled ligand inhibited the rate of dissociation more
(about 10-fold) than theoretically predicted (maximum 2-fold) from
interaction between two similar sites in one macromolecule. A favorable
free energy coupling appeared to exist between the rapid and slow sites but
not between the slow sites. cGMP associated faster to the slow site than
the rapid site. Mg/ATP decreased the rate of association to either site by
50% and increased about ten-fold the rate of dissociation from the slow
site. The dissociation of cGMP from the slow site could be described by a
single activation energy (Ea = 71 kJ X mol-1) for the whole temperature
range (0-37 degrees C) tested. These data indicated that the cyclic
nucleotide-binding sites of the cGMP-kinase are kinetically more homologous
to those in the cAMP-dependent protein kinases than previously recognized.
Studies on the interactions between the cyclic nucleotide-binding sites of cGMP-dependent protein kinase
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