Summary
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1.
Substrates for cAMP-dependent protein kinase were investigated in anterior, intermediate, and neural lobes of the rat pituitary gland. In a cell-free assay system, cAMP increased phosphorylation of 17 K, 33 K, and 60 K macromolecules of the anterior lobe, 17 K, 33 K, 60 K, and 80 K macromolecules of the intermediate lobe, and 60 K, 80 K, and 85 K macromolecules of the neural lobe.
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2.
Other nucleotides were tested in the intermediate lobe; 8 Br-cAMP mimicked cAMP, cGMP was much less effective than cAMP or 8 Br-cAMP, and 5′-AMP showed no significant effect. The purified catalytic subunit of cAMP-dependent protein kinase evoked the same phosphorylation pattern as the endogenous kinase.
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Maximum cAMP-dependent phosphorylation occurred at between 1 and 2 min of incubation; after 20 min, phosphorylation was reduced by 80%. This suggests the presence of phosphatase activity in the intermediate lobe.
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4.
When tested upon dispersed intermediate lobe cells permeabilized by high-voltage electrical discharges, cAMP increased phosphorylation of the 17 K and 33 K macromolecules.
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Furuki, Y., Yamamoto, T., Guild, S. et al. Substrates for adenosine 3′,5′-monophosphate (cAMP)-dependent protein kinase in the rat pituitary gland. Cell Mol Neurobiol 8, 71–83 (1988). https://doi.org/10.1007/BF00712913
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DOI: https://doi.org/10.1007/BF00712913