English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Effect of cytochalasin B on formation and properties of muscle F-actin

MPS-Authors
/persons/resource/persons197059

Löw,  Irmentraut
Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons205722

Dancker,  Peter
Max Planck Institute for Medical Research, Max Planck Society;

Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available
Citation

Löw, I., & Dancker, P. (1976). Effect of cytochalasin B on formation and properties of muscle F-actin. Biochimica et Biophysica Acta: BBA, 430(2), 366-374. doi:10.1016/0005-2728(76)90092-X.


Cite as: http://hdl.handle.net/21.11116/0000-0000-2BC2-5
Abstract
Cytochalasin B stimulated polymerization and decreased the concentration of G-actin remaining in equilibrium with F-actin filaments. Polymerization in the presence of cytochalasin B gave rise to a smaller increase of viscosity but to the same increase in light scattering, compared to polymerization in the absence of cytochalasin B. Cytochalasin B reduced the viscosity of F-actin and caused the appearance of ATP hydrolysis by F-actin. The cytochalasin B-induced ATPase activity was inhibited by concentrations of KCl higher than 50 mM. The cytochalasin B-induced ATPase activity was enhanced by ethyleneglycol bis(α-aminoethyl ether)-N,N′-tetraacetic acid and reduced by MgCl2 at concentrations higher than 0.75 mM. The findings suggest that the stability of actin filaments is reduced by cytochalasin B.