Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
Zur Ablage hinzufügen
  Lokale TagsFreigabegeschichteDetailsÜbersicht

Freigegeben
Zeitschriftenartikel

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

MPG-Autoren
/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;

Externe Ressourcen

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

https://doi.org/10.1016/0005-2728(76)90092-X
(beliebiger Volltext)

Volltexte (beschränkter Zugriff)
Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte in PuRe verfügbar
Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
Zitation

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.


Zitierlink: https://hdl.handle.net/21.11116/0000-0000-2BC2-5
Zusammenfassung
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.