Braginskaya F I, Zorina O M
Institute of Chemical Physics, Academy of Sciences USSR, Moscow.
Radiat Environ Biophys. 1987;26(3):239-49. doi: 10.1007/BF01213710.
Kinetics of erythrocyte acetylcholinesterase activity alterations exposed to ultrasound of therapeutic intensities of 0.88 MHz and 0.05-1.5 W/cm2 was studied. The differences were studied between the mechanisms of the inactivation of membrane-bound and free enzyme: the diminution of active enzyme sites for membrane-bound acetylcholinesterase and the decrease of enzyme-substrate affinity for the free form during sonication. The combined mechanical stresses in the ultrasonic field did not produce inactivation of free enzyme, as compared to the membrane-bound enzyme. Exponential ultrasonic/acoustochemical inactivation curves were obtained for the soluted crystalline form of acetylcholinesterase.
研究了暴露于0.88MHz、0.05 - 1.5W/cm²治疗强度超声下红细胞乙酰胆碱酯酶活性改变的动力学。研究了膜结合酶和游离酶失活机制之间的差异:超声处理期间,膜结合乙酰胆碱酯酶活性位点减少,游离形式的酶 - 底物亲和力降低。与膜结合酶相比,超声场中的复合机械应力未使游离酶失活。获得了乙酰胆碱酯酶溶解结晶形式的指数超声/声化学失活曲线。