Literature DB >> 6679710

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

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

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.

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Year:  1983        PMID: 6679710     DOI: 10.1007/bf02780380

Source DB:  PubMed          Journal:  Appl Biochem Biotechnol        ISSN: 0273-2289            Impact factor:   2.926


  2 in total

1.  Substrate inhibition kinetics in assemblages of cells.

Authors:  B Bunow; C K Colton
Journal:  Biosystems       Date:  1975-07       Impact factor: 1.973

2.  Memory in enzyme membranes.

Authors:  A Naparstek; J L Romette; J P Kernevez; D Thomas
Journal:  Nature       Date:  1974-05-31       Impact factor: 49.962

  2 in total
  1 in total

1.  Modeling the Interaction between β-Amyloid Aggregates and Choline Acetyltransferase Activity and Its Relation with Cholinergic Dysfunction through Two-Enzyme/Two-Compartment Model.

Authors:  Hedia Fgaier; Ibrahim H I Mustafa; Asmaa A R Awad; Ali Elkamel
Journal:  Comput Math Methods Med       Date:  2015-08-30       Impact factor: 2.238

  1 in total

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