We studied the gel-sol transformation of F-actin/alpha-actinin solutions. Cross-linking of actin filaments by alpha-actinin shows a temperature-dependent increase in light scatter signal, (I)T. Higher F-actin/alpha-actinin molar ratios, r(A alpha) as well as increases in F-actin concentration, [A], and reduction of actin filament lengths, rAG, augment the maximal light intensity, I and shift the gel-sol transition point, Tg to higher temperatures. This behavior is interpreted in terms of the model developed by Tempel, M., Isenberg, G. and Sackmann, E. (1996) (Physical Review E 54, 1802-1810) based on the percolation theory. Using the temperature-dependent binding model of this theory allows instant prediction of the equilibrium constant, K for F-actin/alpha-actinin solutions at temperatures T < Tg.
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A nondestructive method to determine viscoelastic properties of gels and fluids involves an oscillating glass fiber serving as a sensor for the viscosity of the surrounding fluid. Extremely small displacements (typically 1-100 nm) are caused by the glass rod oscillating at its resonance frequency. These displacements are analyzed using a phase-sensitive acoustic microscope.
View Article and Find Full Text PDFExamination of temperature-induced 'gel-sol' transformation of alpha-actinin/cross-linked actin networks by static light scattering.
FEBS Lett
April 1998
Surgery Research Laboratories, Massachusetts General Hospital, Harvard Medical School, Charlestown 02129, USA.
We studied the gel-sol transformation of F-actin/alpha-actinin solutions. Cross-linking of actin filaments by alpha-actinin shows a temperature-dependent increase in light scatter signal, (I)T. Higher F-actin/alpha-actinin molar ratios, r(A alpha) as well as increases in F-actin concentration, [A], and reduction of actin filament lengths, rAG, augment the maximal light intensity, I and shift the gel-sol transition point, Tg to higher temperatures.
View Article and Find Full Text PDF[Enhancement of the combination of F-actin and alpha-actinin association in the presence of 1,2-propanediol].
C R Acad Sci III
February 1989
Unité de Recherche en Développement concerté I.N.S.E.R.M.-I.N.R.A. n. 310, Institut de Biologie physico-chimique, Paris.
The influence of 1,2-propanediol on the G-actin/F-actin equilibrium has been studied previously. We report here its effect on the crosslinking of actin filaments by alpha-actinin. Capillary viscometry experiments indicate a marked increase in the viscosity of F-actin/alpha-actinin solutions in the presence of this solvent, with a rise of the gel point temperature.
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