Meerson F Z, Sazontova T G, ARkhipenko Iu V, Kagan V E
Vopr Med Khim. 1986 Sep-Oct;32(5):67-71.
Activity of Na+, K+-ATPase and kinetics of the enzyme thermodenaturation were estimated in preparations of heavy sarcolemma isolated from rat myocardium. Emotional-painful stress (EPS) decreased the enzymatic activity by 20%, whereas the rate of the enzyme thermodenaturation was increased 2-3-fold. A thermodynamic analysis enabled to find a decrease in the energy of activation of the process after the stressory effects as well as alterations in entalpy and entropy under conditions of practically constant changes in free energy; this suggests the possible conformational transformations in the Na+, K+-ATPase molecules in EPS, resembling the state of denaturation. Lipid peroxidation was essential for the decrease in the enzyme thermostability. Activation of lipid peroxidation in the sarcolemma native membranes was accompanied by impairments typical for EPS. Preadministration of an antioxidant ionol before stress protected both the activity and thermostability of Na+, K+-ATPase. Adaptation to EPS by means of multiple short-term stressory actions prevented also the enzyme impairment. Mechanisms of the stress arrhythmogenic effect are discussed.
在从大鼠心肌分离的重肌膜制剂中评估了Na +,K + -ATP酶的活性和酶热变性动力学。情绪性疼痛应激(EPS)使酶活性降低了20%,而酶热变性速率提高了2-3倍。热力学分析能够发现应激效应后该过程的活化能降低,以及在自由能实际恒定变化的条件下焓和熵的变化;这表明EPS中Na +,K + -ATP酶分子可能发生构象转变,类似于变性状态。脂质过氧化对于酶热稳定性的降低至关重要。肌膜天然膜中脂质过氧化的激活伴随着EPS典型的损伤。在应激前预先给予抗氧化剂离子醇可保护Na +,K + -ATP酶的活性和热稳定性。通过多次短期应激作用适应EPS也可防止酶损伤。讨论了应激致心律失常作用的机制。