Unité de Biochimie Cellulaire, Départment de Biochimie et Génétique Moléculaire, Institut Pasteur, 28, rue du Docteur Roux, 75724 Paris Cedex 15, France.
EMBO J. 1982;1(9):1063-8. doi: 10.1002/j.1460-2075.1982.tb01297.x.
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.
我们在分化末期的粘菌细胞中证明了 cAMP 依赖性蛋白激酶的存在。通过亲和层析将 cAMP 结合成分纯化至均质。该亚基抑制来自牛心蛋白激酶的纯化催化亚基的活性；加入 cAMP 后抑制被逆转。该蛋白对 cAMP 具有高度特异性，解离常数为 4 nM。分离的调节亚基是 39 K 的单体，沉降系数为 3.5S，摩擦系数为 1.24。讨论了该调节亚基与其他来源的蛋白激酶的调节亚基之间的差异。
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