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  Analytical solutions of a simple enzyme kinetic problem by a perturbative procedure

Seshadri, M., & Fritzsch, G. (1980). Analytical solutions of a simple enzyme kinetic problem by a perturbative procedure. Biophysics of structure and mechanism, 6(2), 111-123. doi:10.1007/BF00535748.

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 Creators:
Seshadri, M.S.1, Author           
Fritzsch, Günter1, Author           
Affiliations:
1Department of Physical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_3264819              

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Free keywords: Michaelis-Menten kinetics; Singular perturbation; Quasi-steady state; One intermediate product
 Abstract: A systematic perturbative procedure (the method of singular perturbation) is developed to follow the time evolution of an enzyme catalyzed reaction with one intermediate product over the entire time domain of interest. The perturbation parameter is the ratio of the enzyme concentration to the Michaelis-Menten constant. The treatment leads to a meaningful definition of the so-called quasi-steady state often invoked in the description of enzyme catalyzed reactions. The legitimacy and the domain of validity of this assumption are examined in the context of both the reversible and irreversible Michaelis-Menten kinetics.

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Language(s): eng - English
 Dates: 1979-08-301979-10-301980-06-01
 Publication Status: Issued
 Pages: 13
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1007/BF00535748
PMID: 7388120
 Degree: -

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Title: Biophysics of structure and mechanism
  Subtitle : European Biophysics Journal
Source Genre: Journal
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Publ. Info: Berlin : Springer
Pages: - Volume / Issue: 6 (2) Sequence Number: - Start / End Page: 111 - 123 Identifier: ISSN: 0175-7571
CoNE: https://pure.mpg.de/cone/journals/resource/954925487773_1