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  • Title: Diffusion hindrance and geometry of filament crossings account for the complex interactions of F-actin with alpha-actinin from chicken gizzard.
    Author: Grazi E, Cuneo P, Magri E, Schwienbacher C, Trombetta G.
    Journal: Biochemistry; 1993 Aug 31; 32(34):8896-901. PubMed ID: 8395885.
    Abstract:
    The interaction of alpha-actinin from chicken gizzard with F-actin is quite complex. The apparent dissociation constant, C, increases with the increase of actin concentration according to the following expression: C = Ko + a[actin] - c[actin]5/2. At pH 7.5 and 37 degrees C, in the presence of 0.1 M KCl and 2 mM MgCl2, the dissociation constant at infinite actin dilution, Ko, is 2.17 microM. The binding of alpha-actinin to actin is related by the term a[actin] to the diffusion of actin filaments and by the term c[actin]5/2 to the crossing number concentration of the F-actin network. Especially at low actin concentration, the binding of alpha-actinin to actin is increased by gelsolin, which fragments actin filaments and increases their diffusion. The different binding isotherms of alpha-actinin to actin filaments and to actin bundles are discussed.
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