Vergnes H, Moret P R, Duchosal F
Enzyme. 1976;21(1):66-75. doi: 10.1159/000458842.
Exposure of normal rats to chronic natural hypoxia has shown the following effect upon catalytic properties of myocardial lactate dehydrogenase (LDH): significant increase of the two substrates pyruvate and lactate in tissue extracts; no changes in electrophoretic patterns of the enzyme; a slight enhancement of the activation energy of enzyme molecules; a significant increase in the Michaelis constant for pyruvate. Variations in biochemical properties of LDH appear after 12 ueeks of life in high altitude environment. These adjustments may be related to the stimulation of anaerobic metabolism induced by altitudinal hypoxia. Changes in LDH biochemical parameters seem adaptative.
将正常大鼠暴露于慢性自然低氧环境下，已显示出其对心肌乳酸脱氢酶（LDH）催化特性的以下影响：组织提取物中两种底物丙酮酸和乳酸显著增加；酶的电泳图谱无变化；酶分子的活化能略有增强；丙酮酸的米氏常数显著增加。乳酸脱氢酶生化特性的变化在高海拔环境中生活12周后出现。这些调节可能与海拔低氧诱导的无氧代谢刺激有关。乳酸脱氢酶生化参数的变化似乎具有适应性。
