Braginskaya F I, Zaitzeva E A, Zorina O M, Poltorak O M, Chukrai E S, Dunn F
Institute of Chemical Physics, Academy of Sciences USSR, Moscow.
Radiat Environ Biophys. 1990;29(1):47-56. doi: 10.1007/BF01211234.
The kinetics of yeast hexokinase activity exposed to 1 MHz ultrasound of therapeutic intensities 0.1-1.5 W/cm2 was studied using traditional physico-chemical methods and by the thermoinactivation approach. Analysis of the kinetic curves and the kinetic parameters, obtained by two independent methods, suggested specific perturbation processes provoked by the ultrasonic waves, viz., the mechanical breakdown of the contact site between monomer units and the subsequent sonochemical modification of the active enzyme site. Low intensity ultrasound also caused the destabilization of the molecular structure of hexokinase as revealed by the apparent thermolability of the sonicated enzyme.
采用传统物理化学方法和热失活方法，研究了暴露于治疗强度为0.1 - 1.5W/cm²的1MHz超声波下酵母己糖激酶活性的动力学。通过两种独立方法获得的动力学曲线和动力学参数分析表明，超声波引发了特定的扰动过程，即单体单元之间接触位点的机械破坏以及活性酶位点随后的声化学修饰。低强度超声还导致己糖激酶分子结构的不稳定，这通过超声处理后酶的明显热不稳定性得以揭示。
