Gibson D M, Steinrauf J H, Parker R A
J Bioenerg Biomembr. 1984 Dec;16(5-6):433-9. doi: 10.1007/BF00743237.
Steady-state and kinetic equations have been developed which characterize the rates of formation, interconversion, and degradation of an enzyme protein subject to reversible phosphorylation. The theoretical model system incorporates separate fractional degradative rate constants for the phosphorylated and dephosphorylated protein species. The classical models for interconvertible enzymes, and for protein turnover, are special limiting situations of the general model presented here.
已经建立了稳态和动力学方程,这些方程描述了受可逆磷酸化作用的酶蛋白的形成、相互转化和降解速率。该理论模型系统为磷酸化和去磷酸化的蛋白质种类引入了单独的分数降解速率常数。可相互转化酶和蛋白质周转的经典模型是此处提出的通用模型的特殊极限情况。