Literature DB >> 2241989

Microfilament gel rigidity cooperates negatively with the binding of actin gelling proteins.

E Grazi1, G Trombetta, M Guidoboni.   

Abstract

At 37 degrees C, in the presence of 0.1 M KC1 and 2 mM MgCl2, the binding of alpha-actinin to F-actin increases with the concentration of alpha-actinin but not with the concentration of F-actin. This implies that binding is determined by additional factors, beside the alpha-actinin - F-actin association constant. We propose that one of these factors is the rigidity of the gel, which cooperates negatively to the binding by increasing the work needed to bring two actin filaments at the reaction distance with alpha-actinin.

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Year:  1990        PMID: 2241989

Source DB:  PubMed          Journal:  Biochem Int        ISSN: 0158-5231


  2 in total

1.  Binding of alpha-actinin to F-actin or to tropomyosin F-actin is a function of both alpha-actinin concentration and gel structure.

Authors:  E Grazi; G Trombetta; M Guidoboni
Journal:  J Muscle Res Cell Motil       Date:  1991-12       Impact factor: 2.698

2.  alpha-Actinin from chicken gizzard: at low temperature, the onset of actin-gelling activity correlates with actin bundling.

Authors:  E Grazi; G Trombetta; E Magri; P Cuneo; C Schwienbacher
Journal:  Biochem J       Date:  1994-02-15       Impact factor: 3.857

  2 in total

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