Analysis of filamin-actin binding and cross-linking/bundling by kinetic method.
The reaction of smooth muscle filamin and skeletal muscle actin was kinetically examined by double exponential analysis. The overall rate of binding, k+1, is concentration and temperature dependent whilst the overall rate of cross-linking/bundling, k+2, is concentration independent. The activation energy, Ea = 99.5 kJ/mol, was calculated from the Arrhenius Plot.
Goldmann
W H
WH
Technical University of Munich, Garching, FRG.
Senger
R
R
Isenberg
G
G
D000199:Actins / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D000818:Animals; D002151:Calorimetry; D002645:Chickens; D003285:Contractile Proteins / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D003432:Cross-Linking Reagents; D064448:Filamins; D005895:Gizzard, Avian; D007700:Kinetics; D008027:Light; D008840:Microfilament Proteins / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D008854:Microscopy, Electron; D009130:Muscle, Smooth / Q000378:metabolism; D009132:Muscles / Q000378:metabolism; D011485:Protein Binding; D011817:Rabbits; D012542:Scattering, Radiation; D013056:Spectrophotometry, Ultraviolet; D013816:Thermodynamics
D000199:Actins; D003285:Contractile Proteins; D003432:Cross-Linking Reagents; D064448:Filamins; D008840:Microfilament Proteins