Weingand-Ziadé A, Renault F, Masson P
Centre de Recherches du Service de Santé des Armées, Unité de Biochimie, La Tronche, France.
Biochim Biophys Acta. 1997 Jul 18;1340(2):245-52. doi: 10.1016/s0167-4838(97)00051-4.
The combined effects of pressure and temperature on the activity of butyrylcholinesterase (BuChE) were investigated in the pressure range from 10(-3) to 5 kbar and temperature range from -10 degrees C to 70 degrees C. Inactivation of the enzyme showed a complex dependence on pressure and temperature. Under moderate pressures (1-3 kbar) at temperatures 40-65 degrees C BuChE was resistant to heat inactivation; under other conditions of pressure and temperature, the action of both parameters was synergistic and caused inactivation. Results allowed to construct a pressure-temperature kinetic phase diagram for the enzyme inactivation. The elliptic diagram for the irreversible transition active-->inactive BuChE as a function of both pressure and temperature has a positive angular coefficient. This indicates that pressure acts as a stabilizer of BuChE against heat denaturation.
在10⁻³至5千巴的压力范围以及-10℃至70℃的温度范围内，研究了压力和温度对丁酰胆碱酯酶（BuChE）活性的综合影响。酶的失活表现出对压力和温度的复杂依赖性。在40 - 65℃的温度下，中等压力（1 - 3千巴）时，BuChE对热失活具有抗性；在其他压力和温度条件下，这两个参数的作用是协同的，并导致失活。结果使得能够构建酶失活的压力 - 温度动力学相图。作为压力和温度函数的不可逆转变活性→失活BuChE的椭圆形图具有正斜率。这表明压力起到了使BuChE抵抗热变性的稳定剂作用。
