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Actin pp 35-49 | Cite as

Actin-Bound Nucleotide/Divalent Cation Interactions

  • Lewis C. Gershman
  • Lynn A. Selden
  • Henry J. Kinosian
  • James E. Estes
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 358)

Abstract

The protein actin is a major constituent of the cytoskeleton of virtually all eukaryotic cells. The relatively stable actin filament structure of muscle cells is essential to muscle contraction; the motile events of non-muscle cells involve active reorganization of the actin filament network. Actin has binding sites for one tightly bound divalent cation and one adenosine nucleotide per molecule. These ligands are important to the stability of the actin molecule and actin filament, and to the ATP hydrolysis that is involved in actin polymerization in a way which is still incompletely understood.

Keywords

Divalent Cation Nucleotide Binding Nucleotide Exchange Apparent Rate Constant Dissociation Rate Constant 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1994

Authors and Affiliations

  • Lewis C. Gershman
    • 1
    • 2
  • Lynn A. Selden
    • 1
    • 2
  • Henry J. Kinosian
    • 1
    • 2
  • James E. Estes
    • 1
    • 2
  1. 1.Research and Medical ServicesStratton VA Medical CenterAlbanyUSA
  2. 2.Departments of Medicine and Physiology and Cell BiologyAlbany Medical CollegeAlbanyUSA

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