Analysis of filamin and alpha-actinin binding to actin by the stopped flow method

FEBS Lett. 1993 Dec 28;336(3):408-10. doi: 10.1016/0014-5793(93)80847-n.

Abstract

We ascertained by the stopped flow method the overall association rate constant, k+1, of filamin and alpha-actinin to fluorescently labelled filamentous actin of approximately 1.3 x 10(6) M-1.s-1 and approximately 1.0 x 10(6) M-1.s-1 as well as the overall dissociation rate constant, k-1, of approximately 0.6 s-1 and approximately 0.4 s-1, respectively. The overall equilibrium constant, K, for filamin and alpha-actinin to actin deduced from the relation K = k+1/k-1 agree well with published data.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actinin / chemistry*
  • Actinin / metabolism
  • Actins / chemistry*
  • Actins / metabolism
  • Animals
  • Binding, Competitive
  • Carrier Proteins / chemistry
  • Chickens
  • Contractile Proteins / chemistry*
  • Contractile Proteins / metabolism
  • Filamins
  • Gizzard, Avian
  • Kinetics
  • Microfilament Proteins / chemistry*
  • Microfilament Proteins / metabolism
  • Muscle, Smooth / metabolism
  • Muscles / metabolism
  • Rabbits
  • Turkeys

Substances

  • Actins
  • Carrier Proteins
  • Contractile Proteins
  • Filamins
  • Microfilament Proteins
  • Actinin