Literature DB >> 6459679

Cytochalasin B-induced ATPase activity of actin: dependence on monomer concentration.

P Dancker, A Kliche.   

Abstract

We simultaneously measured polymerization and ATPase activity of actin induced by cytochalasin B. It was found that under all conditions tested, ATPase activity was proportional to the concentration of actin which was unpolymerized. In addition, it was found that conditions increasing ATPase activity also increase the velocity of polymerization. From this we conclude that CB-induced ATPase activity is a property of the actin monomers and that the "readiness" of the monomers to hydrolyze ATP is correlated with an increased capacity of the monomers to polymerize.

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Year:  1981        PMID: 6459679     DOI: 10.1515/znc-1981-11-1224

Source DB:  PubMed          Journal:  Z Naturforsch C Biosci        ISSN: 0341-0382


  1 in total

1.  Relation of actin fibrils to energy metabolism of endothelial cells.

Authors:  U Tillmann; J Bereiter-Hahn
Journal:  Cell Tissue Res       Date:  1986       Impact factor: 5.249

  1 in total

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