Evain D, Riou J P, Saez J M
Mol Cell Endocrinol. 1977 Jan;6(3):191-201. doi: 10.1016/0303-7207(77)90085-5.
The protein kinase of normal human adrenal cytosol has been resolved by DEAE-cellulose chromatography into two major components, the protein kinases I and II, which are both adenosine 3',5'-monophosphate (cAMP) dependent. Both enzymes have similar substrate specificities, cAMP-dependency, and sensitivity to the stimulation by this nucleotide, but differ in their states of activation after preincubation with histone. The DEAE--cellulose charomatography of dissociated cytosol protein kinase reveals only one peak of kinase activity and two peaks of cAMP binding activity (A and B). Both binding proteins are able to inhibit the kinase activity of the catalytic subunit. Recombination experiments suggest that the regulatory subunit A originated from protein kinase I and subunit B from protein kinase II. The phosphorylation of histone by adrenal protein kinases is inhibited by a heat-stable protein inhibitor isolated from human fetal brain and human adult adrenal.
正常人肾上腺胞质溶胶的蛋白激酶经二乙氨基乙基纤维素色谱法分离为两个主要成分，即蛋白激酶I和II，二者均依赖于3',5'-环磷酸腺苷（cAMP）。这两种酶具有相似的底物特异性、cAMP依赖性以及对该核苷酸刺激的敏感性，但在用组蛋白预孵育后其激活状态有所不同。解离的胞质溶胶蛋白激酶的二乙氨基乙基纤维素色谱分析仅显示一个激酶活性峰和两个cAMP结合活性峰（A和B）。两种结合蛋白均能抑制催化亚基的激酶活性。重组实验表明，调节亚基A源自蛋白激酶I，亚基B源自蛋白激酶II。人胎儿脑和成人肾上腺中分离出的一种热稳定蛋白抑制剂可抑制肾上腺蛋白激酶对组蛋白的磷酸化作用。
