A cAMP-dependent protein kinase is present in differentiating Dictyostelium discoideum cells
- PMID: 16453431
- PMCID: PMC553163
- DOI: 10.1002/j.1460-2075.1982.tb01297.x
A cAMP-dependent protein kinase is present in differentiating Dictyostelium discoideum cells
Abstract
We demonstrate the occurrence of a cAMP-dependent protein kinase in Dictyostelium discoideum cells at the terminal stage of differentiation. A cAMP-binding component was purified to homogeneity by affinity chromatography. This subunit inhibits the activity of purified catalytic subunit from beef heart protein kinase; the inhibition is reversed upon addition of cAMP. The protein is highly specific for cAMP and has a dissociation constant of 4 nM. The isolated regulatory subunit is a monomer of 39 K, with a sedimentation coefficient of 3.5S and a frictional coefficient of 1.24. The differences between this regulatory subunit and regulatory subunits of protein kinases from other sources are discussed.
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