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 language | English |
|---|---|
| Pages (from-to) | 633-640 |
| Number of pages | 8 |
| Journal | Biochemistry International |
| Volume | 21 |
| Issue number | 4 |
| Publication status | Published - 1990 |
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- 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 journal › Article
}
TY - JOUR
T1 - Microfilament gel rigidity cooperates negatively with the binding of actin gelling proteins
AU - Grazi, E.
AU - Trombetta, G.
AU - Guidoboni, M.
PY - 1990
Y1 - 1990
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0025029785&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0025029785&partnerID=8YFLogxK
M3 - Article
VL - 21
SP - 633
EP - 640
JO - Biochemistry and Molecular Biology International
JF - Biochemistry and Molecular Biology International
SN - 1039-9712
IS - 4
ER -