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Examination of temperature‐induced ‘gel‐sol’ transformation of α‐actinin/cross‐linked actin networks by static light scattering
Author(s) -
Goldmann Wolfgang H.,
Guttenberg Zeno
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00353-6
Subject(s) - actin , protein filament , actinin , chemistry , actina , materials science , biophysics , crystallography , cytoskeleton , biology , biochemistry , cell
We studied the gel‐sol transformation of F‐actin/α‐actinin solutions. Cross‐linking of actin filaments by α‐actinin shows a temperature‐dependent increase in light scatter signal, ( I ) T . Higher F‐actin/α‐actinin molar ratios, r Aα as well as increases in F‐actin concentration, [A], and reduction of actin filament lengths, r AG , augment the maximal light intensity, I and shift the gel‐sol transition point, T g 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/α‐actinin solutions at temperatures T < T g .