通过稀释共价修饰蛋白进行再生的动力学分析。
Kinetic analysis of regeneration by dilution of a covalently modified protein.
作者信息
Rakitzis E T
机构信息
Department of Biological Chemistry, University of Athens Medical School, Greece.
出版信息
Biochem J. 1990 Jun 15;268(3):669-70. doi: 10.1042/bj2680669.
An analysis of regeneration by dilution of a covalently modified protein is presented. It is shown that, when protein regeneration is realized through the intermediacy of a protein-modifying agent adsorptive complex, the reaction is described by a summation of two exponential functions of reaction time plus a constant-term equation. The conditions whereby this equation reduces to a single-exponential equation are delineated. It is shown that, when protein regeneration is described by a single-exponential function of reaction time, the first-order protein-regeneration rate constant is a function of modifying-agent concentration and also of the microscopic reaction rate constants. Accordingly, the protein-modifying agent dissociation constant (Ki), as well as the protein-covalent-modification and -regeneration, rate constants (k+2 and K-2), may be determined by an analysis of dilution-induced protein-regeneration (or enzyme-reactivation) data obtained at different dilutions of the covalently modified protein-modifying agent preparation.
本文对通过稀释共价修饰蛋白质实现的再生进行了分析。结果表明，当蛋白质再生通过蛋白质修饰剂吸附复合物介导实现时，该反应可由反应时间的两个指数函数之和加上一个常数项方程来描述。阐述了该方程简化为单指数方程的条件。结果表明，当蛋白质再生由反应时间的单指数函数描述时，一级蛋白质再生速率常数是修饰剂浓度以及微观反应速率常数的函数。因此，蛋白质修饰剂解离常数（Ki）以及蛋白质共价修饰和再生速率常数（k+2和K-2）可通过分析在共价修饰蛋白质修饰剂制剂的不同稀释度下获得的稀释诱导蛋白质再生（或酶再活化）数据来确定。
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