Random copolymerization of ATP-actin and ADP-actin.
The equilibrium of the copolymerization of ATP-actin and ADP-actin was investigated by an analysis of the critical concentrations of mixtures of ATP-actin and ADP-actin. The molar ratio of bound ATP to bound ADP was controlled by the ratio of free ATP and ADP. The experiments were performed under conditions (100 mM KCl, l mM MgCl2, pH 7.5, 25 degrees C) where the ATP hydrolysis following binding of actin monomers to barbed filament ends was so slow that the distribution of ATP or ADP bound to the subunits near the ends of filaments was not affected by ATP hydrolysis. According to the analysis of the critical concentrations, the equilibrium constants for incorporation of ATP-actin or ADP-actin into filaments were independent of the type of nucleotide bound to contiguous subunits.
Ohm
T
T
Institute of Physiological Chemistry, Ruhr-University, Bochum, Federal Republic of Germany.
Wegner
A
A
D000199:Actins / Q000378:metabolism*; D000244:Adenosine Diphosphate / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D004985:Ethenoadenosine Triphosphate / Q000378:metabolism; D007700:Kinetics; D046911:Macromolecular Substances; D008433:Mathematics; D008954:Models, Biological; D009132:Muscles / Q000378:metabolism; D011485:Protein Binding; D011817:Rabbits; D013050:Spectrometry, Fluorescence
D000199:Actins; D004985:Ethenoadenosine Triphosphate; D046911:Macromolecular Substances; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate