   3.1.1.7 | -999 |
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kinetics of thermal denaturation of acetylcholinesterase of the rat red blood cell membrane during moderate hypothermia, thermostability of acetylcholinesterase of rat erythrocyte membranes in the norm and moderate hypothermia, detailed overview. Kinetics of the thermal denaturation of acetylcholinesterase are nonlinear and correspond to a model that involves two-step denaturation, fast and slow, of the enzyme's native form. The rate constants of the fast phase, k1, are much higher than those of the slow phase, k2, while the energy of the fast phase activation is lower by only 19.4% compared to that of the slow one. Short-term moderate hypothermia increases k1 and decreases the index of relative activity of the intermediate form of acetylcholinesterase (parameter beta), leading to significant lowering of the activation energies of both stages, parameter beta becomes more temperature-dependent. The prolongation of hypothermia up to 3 h mainly contributes to a decrease in k1 and k2 relative to short-term hypothermia and the activation energy of denaturation increases. The structure of acetylcholinesterase is labilized at the initial stages of the development of the hypothermic state and stabilized during prolonged hypothermia. Molecular mechanisms of the changes in the thermal stability of erythrocyte AChE |
750070 |
