Thermostability of Lactate Dehydrogenase in Rat Brain under Conditions of Short-Term Moderate Hypothermia.

Thermostability of rat brain lactate dehydrogenase (LDH) was studied in intact animals and animals subjected to moderate short-term hypothermia. Two exponential stages, rapid and slow, were distinguished in the thermodenaturation kinetics. The contribution of the rapid phase to the lactate dehydrogenase denaturation kinetics was more significant: the energy of activation for this phase was 2.33 times lower than that for the slow phase. Moderate shortterm hypothermia led to a significant decrease of lactate dehydrogenase thermostability: thermodenaturation rate constants for the rapid (k1) and slow (k2) phases increased. Significant changes in parameters a and b reflecting the initial proportion of the two native forms of the enzyme developed only at 40°C. As hypothermia caused no appreciable changes in the energy of activation of lactate dehydrogenase denaturation, a significant contribution of the entropic factor to the decrease of free energy of enzyme denaturation was hypothesized. The data indicated significant labilization of lactate dehydrogenase structure under conditions of moderate hypothermia.