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Titlebook: Kinetics of Enzyme-Modifier Interactions; Selected Topics in t Antonio Baici Book 2015 Springer-Verlag Wien 2015 Activation.Enzyme kinetics

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31#
發(fā)表于 2025-3-26 23:51:28 | 只看該作者
,Taxonomy of Enzyme–Modifier Interactions and the Specific Velocity Plot,inations that are assigned to individual kinetic mechanisms embracing inhibition and nonessential activation. Essential activation is ranked as a separate group. The specific velocity plot, a method based on the same basic characters used in taxonomy, is exploited for the differential diagnosis of mechanisms during data analysis.
32#
發(fā)表于 2025-3-27 02:37:24 | 只看該作者
33#
發(fā)表于 2025-3-27 07:17:29 | 只看該作者
Enzyme Inactivation with a Note on the Significance of Slow Modification Processes,ty to the interpretation of raw data. This chapter discusses the strategies that can be exploited to recognize and interpret enzyme inactivation in the presence of unstable modifiers and of modifiers with substrate-like properties.
34#
發(fā)表于 2025-3-27 13:14:56 | 只看該作者
35#
發(fā)表于 2025-3-27 14:35:54 | 只看該作者
36#
發(fā)表于 2025-3-27 20:28:15 | 只看該作者
Multiple Enzyme-Modifier Interactions,ation resulting from the combination of two inhibitors and efficient inhibition ensuing from the concomitant action of two nonessential activators, have a defined mechanistic meaning and embody sophisticated regulatory strategies.
37#
發(fā)表于 2025-3-27 23:10:02 | 只看該作者
Dichotomous Keys to Enzyme-Modification Mechanisms,imen to a family, genus, and finally to a species. This task, which consists in evaluating all elements available and in analyzing them until finding a unique combination of traits, is facilitated by the use of diagnostic keys. The dichotomous keys in this chapter aim at supporting the identification of kinetic mechanisms of enzyme modifiers.
38#
發(fā)表于 2025-3-28 05:58:18 | 只看該作者
39#
發(fā)表于 2025-3-28 06:58:07 | 只看該作者
40#
發(fā)表于 2025-3-28 11:57:36 | 只看該作者
Multiple Interactions: Essential Activation and Liberation,ivator. The mechanisms of action of the liberator, a substance that reverts inhibition or activation by any modifier, can optimally be understood and interpreted using the formalism of multiple enzyme-modifier interactions.
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