Analysis of filamin and alpha-actinin binding to actin by the stopped flow method.
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.
Goldmann
W H
WH
Technical University of Munich, Department of Biophysics, Garching, Germany.
Isenberg
G
G
D000185:Actinin / Q000737:chemistry* / Q000378:metabolism; D000199:Actins / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D001667:Binding, Competitive; D002352:Carrier Proteins / Q000737:chemistry; D002645:Chickens; D003285:Contractile Proteins / Q000737:chemistry* / Q000378:metabolism; D064448:Filamins; D005895:Gizzard, Avian; D007700:Kinetics; D008840:Microfilament Proteins / Q000737:chemistry* / Q000378:metabolism; D009130:Muscle, Smooth / Q000378:metabolism; D009132:Muscles / Q000378:metabolism; D011817:Rabbits; D014422:Turkeys
D000199:Actins; D002352:Carrier Proteins; D003285:Contractile Proteins; D064448:Filamins; D008840:Microfilament Proteins; D000185:Actinin