Kinetic analysis of the polymerization process of actin.
The polymerization process of actin was examined by measuring the amount of flow birefringence and by analyzing release of labeled inorganic phosphate from the bound [gamma-32P]ATP upon polymerization of G-actin to F-actin. Comparison of the above experimental results with the electron microscopic data of Kawamura and Maruyama (J. Biochem., 67, 437-457, 1970) suggested that growth and redistribution steps occurred simultaneously during polymerization. Attempt was made to simulate the polymerization process of actin by calculating the kinetic equations numerically. The results of simulation suggested that it was necessary to take into consideration the association and dissociation between F-actin particles as well as the association and dissociation between F-actin and G-actin.
D000199:Actins; D000255:Adenosine Triphosphate / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D001718:Birefringence; D007700:Kinetics; D046911:Macromolecular Substances; D008433:Mathematics; D009132:Muscles; D010710:Phosphates / Q000032:analysis; D011485:Protein Binding; D011817:Rabbits
D000199:Actins; D046911:Macromolecular Substances; D010710:Phosphates; D000255:Adenosine Triphosphate