[Possible role of structural changes in ATP hydrolysis by subfragment-1 and myosin].
Dependence of the rate of ATP hydrolysis with subfragment-I and temperature of SF-I, denaturation on the concentration of heavy water in solution was studied. The value of kinetic isotope effect V/Vx linearly increases with the rise of the volume portion of heavy water in solution and at X-1 it equals 1.9. The temperature of protein denaturacticn increases with X rise, the pattern of this relationship looking as an arched curve. The results differ from those earlier obtained on myosin which points to the absence of essential contribution of structural dynamic changes to enzymic hydrolysis of ATP by subfragment-I.
D000255:Adenosine Triphosphate / Q000378:metabolism; D007700:Kinetics; D015879:Myosin Subfragments; D009218:Myosins / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism*
D015879:Myosin Subfragments; D010446:Peptide Fragments; D000255:Adenosine Triphosphate; D009218:Myosins
O vozmozhnoĭ roli fluktuatsiĭ struktury pri gidrolize ATF subfragmentom-1 i miozinom.