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Analysis of filamin and α‐actinin binding to actin by the stopped flow method
Author(s) -
Goldmann W.H.,
Isenberg G.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80847-n
Subject(s) - filamin , actinin , actin , actina , dissociation constant , reaction rate constant , chemistry , constant (computer programming) , equilibrium constant , biophysics , biochemistry , biology , physics , cytoskeleton , kinetics , receptor , computer science , cell , programming language , quantum mechanics
We ascertained by the stopped flow method the overall association rate constant, k +1 , of filamin and α‐actinin to fluorescently labelled filamentous actin of ~ 1.3 × 10 6 M −1 · s −1 and ~ 1.0 × 10 6 M −1 · s −1 as well as the overall dissociation rate constant, k −1 of ~ 0.6s −1 and ~ 0.4s −1 , respectively. The overall equilibrium constant, K , for filamin and α‐actinin to actin deduced from the relation K = agree well with published data.