English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
  Local TagsRelease HistoryDetailsSummary

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;

External Resource

https://www.sciencedirect.com/science/article/pii/000527287690092X/pdf?md5=c221a368701d2bc290db440a3cdcba8f&pid=1-s2.0-000527287690092X-main.pdf
(Any fulltext)

https://doi.org/10.1016/0005-2728(76)90092-X
(Any fulltext)

Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
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: https://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.