Abduragimov A R, Tiurkin V V, Kochetkov S N, Severin E S
Biokhimiia. 1986 Nov;51(11):1886-92.
Modification of the holoenzyme of cAMP-dependent protein kinase from porcine brain by dimethylsuberimidate was studied. It was demonstrated that a protein conjugate with a molecular mass of 180,000 Da and a stoichiometric formula of R2C2 evolves as a result of intermolecular cross-link formation in the holoenzyme molecule. The regulatory subunit partly protects the catalytic subunit from the inhibition by dimethylsuberimidate. The cross-linked holoenzyme retains the ability to be activated by cAMP. The experimental data testify to the non-identity of activation and dissociation of protein kinase.
研究了用二甲基辛二亚胺对猪脑cAMP依赖性蛋白激酶全酶的修饰作用。结果表明，由于全酶分子中分子间交联的形成，产生了一种分子量为180,000 Da、化学计量式为R2C2的蛋白质缀合物。调节亚基部分保护催化亚基免受二甲基辛二亚胺的抑制。交联的全酶保留了被cAMP激活的能力。实验数据证明蛋白激酶的激活和解离并非同一过程。
