Analysis of filamin and α‐actinin binding to actin by the stopped flow method

FEBS Letters

Isenberg, G.¹  Goldmann, W.H.¹ 

[1] Technical University of Munich, Department of Biophysics, E22, D-85747 Garching, Germany

关键词: Actin;    Filamin;    α-Actinin;    Transient kinetics;   

DOI  :  10.1016/0014-5793(93)80847-N

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 × 10⁶M⁻¹ · s⁻¹ and ~ 1.0 × 10⁶M⁻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.

【 授权许可】

Unknown