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

E. Grazi, G. Trombetta, M. Guidoboni

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

At 37°C, in the presence of 0.1 M KCl 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.

Original languageEnglish
Pages (from-to)633-640
Number of pages8
JournalBiochemistry International
Volume21
Issue number4
Publication statusPublished - 1990

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Actinin
Microfilament Proteins
Actin Cytoskeleton
Rigidity
Actins
Gels
Magnesium Chloride

ASJC Scopus subject areas

  • Biochemistry

Cite this

Microfilament gel rigidity cooperates negatively with the binding of actin gelling proteins. / Grazi, E.; Trombetta, G.; Guidoboni, M.

In: Biochemistry International, Vol. 21, No. 4, 1990, p. 633-640.

Research output: Contribution to journalArticle

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