Phalloidin Binding and Rheological Differences among Actin Isoforms

• Published in: Biochemistry (Easton) Vol. 35; no. 45; pp. 14062 - 14069
• Main Authors: Allen, P. G, Shuster, C. B, Käs, J, Chaponnier, C, Janmey, P. A, Herman, I. M
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 12.11.1996
• Subjects: Actins - chemistry; Animals; Cattle; Cell-Free System; Chickens; Elasticity; Kinetics; Models, Molecular; Muscle, Skeletal - chemistry; Muscle, Smooth - chemistry; Phalloidine - chemistry; Protein Structure, Tertiary; Rabbits; Rheology; Saccharomyces cerevisiae; Structure-Activity Relationship; Viscosity

Actin is a highly conserved protein in eukaryotes, yet different isoforms of this protein can be found within the same cell. To begin to explore whether isoactin sequence diversity leads to functional differences in actin filaments, we have examined the phalloidin binding kinetics and the bulk rheol...