[Mechanochemical interactions in enzymes. IV. Mechanochemical properties of immobilized preparations of F-actin].
Oriented immobilized F-actin (IA) threads were prepared by extrusion of the concentrated F-actin solutions through a capillar into an aceton-water mixture containing glutaraldehyde. Myosin ATP-ase activity was activated by IA in the presence of Mg+2 and inhibited in the presence of EDTA. ATPase activity of IA at high temperature (55) was about 0.054 min(-1) and was not affected by a deformation of threads. Mechanical properties of IA threads were changed when treated by reagnets influencing intra- and inter-molecular interactions of actin molecules, and these changes themselves were highly dependent on IA threads deformation.
D000199:Actins; D000251:Adenosine Triphosphatases; D004492:Edetic Acid; D008274:Magnesium; D009218:Myosins
D000199:Actins; D004492:Edetic Acid; D000251:Adenosine Triphosphatases; D009218:Myosins; D008274:Magnesium
Mekhanokhimicheskie vazimodeĭstviia v fermentakh. IV. Mekhanokhimicheskie svoĭstva immobilizovannykh preparatov F-aktina