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The effect of hydrogen ion on the steady-state multiplicity of substrate-inhibited enzymatic reactions. II. Transient behavior.

作者信息

Elnashaie S S, Elrifaie M A, Ibrahim G, Badra G

出版信息

Appl Biochem Biotechnol. 1983 Dec;8(6):467-79. doi: 10.1007/BF02780380.

DOI:10.1007/BF02780380
PMID:6679710
Abstract

In this paper we concentrate our attention on the stability and transient behavior of the isothermal system (CSTR) with a substrate-inhibited enzyme reaction producing hydrogen ions. Our investigation covers the region of multiple steady states uncovered previously (1) (ordinary hysteresis and isola). We investigate the local stability characteristics of the different steady states, the effect of the initial condition on the transient behavior and the response of the system to feed disturbances of various magnitudes and durations.

摘要

相似文献

1
The effect of hydrogen ion on the steady-state multiplicity of substrate-inhibited enzymatic reactions. II. Transient behavior.
Appl Biochem Biotechnol. 1983 Dec;8(6):467-79. doi: 10.1007/BF02780380.
2
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Modeling the Interaction between β-Amyloid Aggregates and Choline Acetyltransferase Activity and Its Relation with Cholinergic Dysfunction through Two-Enzyme/Two-Compartment Model.通过双酶/双室模型模拟β-淀粉样蛋白聚集体与胆碱乙酰转移酶活性之间的相互作用及其与胆碱能功能障碍的关系。
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本文引用的文献

1
Memory in enzyme membranes.酶膜中的记忆。
Nature. 1974 May 31;249(456):490-1. doi: 10.1038/249490a0.
2
Substrate inhibition kinetics in assemblages of cells.细胞集合体中的底物抑制动力学。
Biosystems. 1975 Jul;7(1):160-71. doi: 10.1016/0303-2647(75)90054-4.