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  A kinetic analysis of enzyme inactivation as applied to the covalent modification of Na+ + K+-ATPase and Ca2+-ATPase

Fritzsch, G. (1985). A kinetic analysis of enzyme inactivation as applied to the covalent modification of Na+ + K+-ATPase and Ca2+-ATPase. Journal of Theoretical Biology, 117(3), 397-415. doi:10.1016/S0022-5193(85)80151-X.

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

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 Abstract: A kinetic analysis of enzyme inactivation due to the covalent binding of chemically modified ligands is presented. Reaction schemes similar to the Michaelis-Menten scheme have been studied as well as schemes with two states of the enzyme or two binding sites. The resulting kinetic equations lead to time courses of inactivation which can be represented by two exponential functions at least in a quasi-steady state approximation. These curves are frequently encountered in inactivation experiments. Since rapid methods for model selection and parameter estimation are desirable, but not available, a technique for a preliminary analysis of the experimental data is presented. A mere glance at the time courses shows what reaction schemes are inapplicable. For each family of inactivation curves, the construction of a line of intersections is proposed. This line contains essential kinetic information and can further be utilized for a rough parameter estimation. The technique is illustrated for three sets of experimental data where Na+ + K+-ATPase and Ca2+-ATPase have been inactivated by ATP-analogs.

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Language(s): eng - English
 Dates: 1985-07-101985-01-192006-07-141985-12-07
 Publication Status: Issued
 Pages: 19
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/S0022-5193(85)80151-X
PMID: 3007869
 Degree: -

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Title: Journal of Theoretical Biology
  Abbreviation : J. Theor. Biol.
Source Genre: Journal
 Creator(s):
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Publ. Info: London : Elsevier
Pages: - Volume / Issue: 117 (3) Sequence Number: - Start / End Page: 397 - 415 Identifier: ISSN: 0022-5193
CoNE: https://pure.mpg.de/cone/journals/resource/954922646048