Combined pressure/heat-induced inactivation of butyrylcholinesterase.
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.
Weingand-Ziadé
A
A
Centre de Recherches du Service de Santé des Armées, Unité de Biochimie, La Tronche, France.
Renault
F
F
Masson
P
P
D002091:Butyrylcholinesterase / Q000737:chemistry / Q000378:metabolism*; D004789:Enzyme Activation; D006358:Hot Temperature; D006801:Humans; D007700:Kinetics; D011312:Pressure; D011489:Protein Denaturation; D013816:Thermodynamics
D002091:Butyrylcholinesterase