Gabibov A G, Kochetkov S N, Sashchenko L P, Smirnov I V, Timofeev V P, Severin E S
Eur J Biochem. 1983 May 2;132(2):339-44. doi: 10.1111/j.1432-1033.1983.tb07367.x.
The interaction of the cAMP-dependent protein kinase catalytic subunit with its protein substrate, histone H1, was studied. The H1 molecule was specifically converted into the aminotyrosine-72 derivative. Fluorescent and spin labels were introduced into this residue. The changes in the ESR and fluorescence spectra of respective derivatives were observed upon the interaction of the latter with the catalytic subunit, thus enabling us to determine some kinetic and equilibrium parameters of this process. Stopped-flow investigation of the transient phase of the binding reaction indicates that the kinetic curve is described by a three-exponential function. The rate of protein-protein interaction is close to the rate of phosphate transfer from phosphoenzyme intermediate to protein substrate.
研究了环磷酸腺苷（cAMP）依赖性蛋白激酶催化亚基与其蛋白底物组蛋白H1的相互作用。H1分子被特异性转化为氨基酪氨酸-72衍生物。将荧光和自旋标记引入该残基。当后者与催化亚基相互作用时，观察到相应衍生物的电子自旋共振（ESR）和荧光光谱的变化，从而使我们能够确定该过程的一些动力学和平衡参数。对结合反应瞬态阶段的停流研究表明，动力学曲线由三指数函数描述。蛋白质-蛋白质相互作用的速率接近于磷酸从磷酸酶中间体转移到蛋白质底物的速率。
