title: Examination of temperature-induced 'gel-sol' transformation of alpha-actinin/cross-linked actin networks by static light scattering.
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.
authors.affiliation: Surgery Research Laboratories, Massachusetts General Hospital, Harvard Medical School, Charlestown 02129, USA. goldman@helix.mgh.harvard.edu
authors.forename: W H
authors.initials: WH
authors.lastname: Goldmann
authors.forename: Z
authors.initials: Z
authors.lastname: Guttenberg
mesh_terms: D000185:Actinin / Q000737:chemistry*; D000199:Actins / Q000737:chemistry*; D000818:Animals; D002474:Cell-Free System; D005782:Gels; D007700:Kinetics; D008027:Light; D046911:Macromolecular Substances; D011817:Rabbits; D012542:Scattering, Radiation; D013696:Temperature; D014422:Turkeys
chemical_list: D000199:Actins; D005782:Gels; D046911:Macromolecular Substances; D000185:Actinin