Kinetics of protein modification, and/or enzyme inactivation, reactions by an unstable modifying agent.
作者信息
Rakitzis E T
出版信息
Biochem J. 1987 Sep 15;246(3):803-5. doi: 10.1042/bj2460803.
Abstract
摘要
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Kinetics of protein modification, and/or enzyme inactivation, reactions by an unstable modifying agent.不稳定修饰剂引发的蛋白质修饰和/或酶失活反应的动力学
Biochem J. 1987 Sep 15;246(3):803-5. doi: 10.1042/bj2460803.
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The equilibrium assumption is valid for the kinetic treatment of most time-dependent protein-modification reactions.平衡假设对于大多数随时间变化的蛋白质修饰反应的动力学处理是有效的。
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Utilization of the free energy of the reversible binding of protein and modifying agent towards the rate-enhancement of protein covalent modification.利用蛋白质与修饰剂可逆结合的自由能来提高蛋白质共价修饰的速率。
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Alternative methods for the determination of rate constants describing enzyme inactivation by an unstable inhibitor.测定不稳定抑制剂使酶失活的速率常数的替代方法。
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Kinetic analysis of modification reactions at comparable enzyme and modifier concentrations.在可比的酶和修饰剂浓度下修饰反应的动力学分析。
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Kinetics of protein-modification reactions. Determination of the fractional concentration of enzyme protein groups, or group reactivities, essential for catalytic function.蛋白质修饰反应的动力学。催化功能所必需的酶蛋白基团的分数浓度或基团反应性的测定。
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Experimental approach to the kinetic study of unstable site-directed irreversible inhibitors: kinetic origin of the apparent positive co-operativity arising from inactivation of trypsin by p-amidinophenylmethanesulphonyl fluoride.不稳定的定点不可逆抑制剂动力学研究的实验方法：对氨基苯甲脒基甲磺酰氟使胰蛋白酶失活产生的表观正协同性的动力学起源
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Alternative methods for the determination of rate constants describing enzyme inactivation by an unstable inhibitor.测定不稳定抑制剂使酶失活的速率常数的替代方法。
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Comments on the kinetic analysis of enzyme reactions involving an unstable irreversible modifier.关于涉及不稳定不可逆修饰剂的酶反应动力学分析的评论
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