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PMID: 2241989 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

Biochemistry international ·Vol. 21 ·No. 4 ·1990-00-00 ·Pages 633-40

Grazi E, Trombetta G, Guidoboni M

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.

MeSH Terms
Actin Cytoskeleton/metabolism Actinin/chemistry,metabolism Actins/metabolism Animals Gels In Vitro Techniques Microfilament Proteins/chemistry,metabolism
Chemicals
Actins Gels Microfilament Proteins Actinin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Grazi E
Istituto di Chimica Biologica, Universita di Ferrara, Italy.
Trombetta G
Guidoboni M
Article Info
Journal
Biochemistry international
Abbr.
Biochem Int
ISSN
0158-5231
Published
1990-00-00
Pages
633-40
Language
English
Region
Australia
NLM ID
8100311
Subset
IM
External Links
PubMed source
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