title: Preferential binding of alpha-actinin to actin bundles.
abstract: At 37 degrees C, the alpha-actin-F-actin binding isotherm is anomalous. In 6.7% polyethylene glycol 6000, concomitantly with the formation of actin bundles, the binding isotherm becomes hyperbolic (Kdiss. = 11.3 microM). alpha-Actinin increases the rigidity of the networks formed by actin bundles in polyethylene glycol and by paracrystalline actin in 16 mM MgCl2 but not by F-actin. It is proposed that in the cell alpha-actinin functions are mostly carried on by interaction with actin bundles.
authors: Istituto di Chimica Biologica, Università di Ferrara, Italy.
authors: E
authors: E
authors: Grazi
authors: P
authors: P
authors: Cuneo
authors: E
authors: E
authors: Magri
authors: C
authors: C
authors: Schwienbacher
mesh_terms: D000185:Actinin / Q000378:metabolism*; D000199:Actins / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D003461:Crystallography; D015636:Magnesium Chloride / Q000494:pharmacology; D011092:Polyethylene Glycols / Q000494:pharmacology; D011817:Rabbits
chemical_list: D000199:Actins; D015636:Magnesium Chloride; D000185:Actinin; D011092:Polyethylene Glycols