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  Kinetics and mechanism of cation-binding to Na+,K+-ATPase

Doludda, M., Lewitzki, E., Ruf, H., & Grell, E. (1994). Kinetics and mechanism of cation-binding to Na+,K+-ATPase. In E. Bamberg, & W. Schoner (Eds.), The Sodium Pump (pp. 629-632). Darmstadt, Germany: Dietrich Steinkopff Verlag GmbH & Co. KG, Darmstadt 1994.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0007-FD86-5 Version Permalink: https://hdl.handle.net/21.11116/0000-0007-FD87-4
Genre: Book Chapter

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 Creators:
Doludda, Michael1, Author           
Lewitzki, Erwin1, Author           
Ruf, Horst1, Author           
Grell, Ernst1, Author           
Affiliations:
1Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              

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Free keywords: Choline Chloride; Selective Binding; Cation Binding; Saturation Behaviour; High Affinity Binding Site
 Abstract: Most mechanistic aspects of cation binding and transport by Na+K+-ATPase are still unknown. The kinetics of cation binding with the FTTC-enzyme can be studied using the stopped flow technique (1,3,4) taking advantage of the large fluorescence intensity changes caused by these reactions (1,2). In contrast to equilibrium titration experiments, kinetic studies can provide evidence for the existence of intermediate states.

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Language(s): eng - English
 Dates: 1994
 Publication Status: Issued
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1007/978-3-642-72511-1_113
 Degree: -

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Title: The Sodium Pump
  Subtitle : Structure Mechanism, Hormonal Control and its Role in Disease
Source Genre: Book
 Creator(s):
Bamberg, Ernst1, Editor           
Schoner, Wilhelm2, Editor
Affiliations:
1 Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289            
2 Institut für Biochemie, Universität Gießen, Gießen, Germany, ou_persistent22            
Publ. Info: Darmstadt, Germany : Dietrich Steinkopff Verlag GmbH & Co. KG, Darmstadt 1994
Pages: 906 Volume / Issue: - Sequence Number: - Start / End Page: 629 - 632 Identifier: DOI: 10.1007/978-3-642-72511-1
ISBN: 978-3-642-72513-5
ISBN: 978-3-642-72511-1