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J. Biol. Chem., Vol. 255, Issue 24, 11768-11774, 12, 1980
JR Vandenheede, SD Yang, J Goris and W Merlevede
A protein (FA) has been isolated from rabbit muscle which has two
functions: one is the activation of the ATP x Mg-dependent phosphatase (see
previous paper) (1) and the second is the phosphorylation and concomitant
inactivation of glycogen synthase, independent from cyclic AMP or Ca ions.
The two activities co-purify throughout the purification scheme, and reside
in the single protein band that the purified preparation shows in
discontinuous acrylamide gel electrophoresis. Heat inactivation experiments
with the purified protein showed a parallel decrease of both activities
with time. GTP could efficiently replace the ATP in both reactions. Sodium
dodecyl sulfate-gel electrophoresis also shows a single protein-stained
band corresponding to a Mr = approximately 50,000 and sucrose density
gradient centrifugation gave a value of 45,000. The enzyme incorporates
only 1 mol of phosphate/mol of synthase monomer (85,000 daltons) and brings
the activity ratio (+/- glucose-6-P) down to less than 0.05. Kinetic
studies suggest that FA exerts its two activities in quite different ways:
the activation of the ATP x Mg-dependent phosphatase is bought about by a
protein-protein interaction (FA x FC complex formation) with ATP x Mg as a
necessary cofactor, whereas for the inactivation of synthase, FA is a
cyclic AMP- and Ca-independent kinase.
ATP x Mg-dependent protein phosphatase from rabbit skeletal muscle. II. Purification of the activating factor and its characterization as a bifunctional protein also displaying synthase kinase activity
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