Artiukhov V G, Nakvasina M A, Popova V V
Biofizika. 1994 Jul-Aug;39(4):576-82.
Structural and functional properties of the lactate dehydrogenase modified by temperature at range 40-70 degrees C have been investigated. Kinetic principles of the thermoinactivation have been studied. The rate constants and the activation energy have been determined. Analysis of changes of the protein molecular mass leads to the conclusion that high-temperature denaturation of the lactate dehydrogenase (in investigated temperature interval) depends on oligomer molecule dissociation to monomers and subsequent aggregation of protein subunits.
研究了在40-70摄氏度范围内温度对乳酸脱氢酶结构和功能特性的影响。研究了热失活的动力学原理。测定了速率常数和活化能。对蛋白质分子量变化的分析得出结论，乳酸脱氢酶的高温变性（在所研究的温度区间内）取决于寡聚体分子解离为单体以及随后蛋白质亚基的聚集。
