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. 1998 Apr 17;426(2):255-9.
doi: 10.1016/s0014-5793(98)00353-6.

Examination of temperature-induced 'gel-sol' transformation of alpha-actinin/cross-linked actin networks by static light scattering

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Examination of temperature-induced 'gel-sol' transformation of alpha-actinin/cross-linked actin networks by static light scattering

W H Goldmann et al. FEBS Lett. .
Free article

Abstract

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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