Volmer H, Veltel D
Comp Biochem Physiol A Comp Physiol. 1985;81(4):761-8. doi: 10.1016/0300-9629(85)90906-5.
The temperature dependence of delipidated and phospholipid-replaced ATPase from crayfish and locust sarcoplasmic reticulum (SR) was studied. Removal of approx. 85% of the phospholipids present in locust SR considerably decreased the temperature optimum of the ATPase, indicating that the thermostability of the ATPase is dependent on the phospholipids surrounding the enzyme. Addition of distearoylphosphatidylcholine to the delipidated ATPase from locust and crayfish SR increased the thermostability, whereas a decrease could be observed upon addition of dilinoleoyl- and dimyristoylphosphatidylcholine. These results suggest that the thermostability of the ATPase might be affected by the conformation of the fatty acyl chains in the microenvironment of the enzyme.
研究了小龙虾和蝗虫肌浆网（SR）中脱脂及磷脂替代的ATP酶的温度依赖性。去除蝗虫SR中约85%的磷脂会显著降低ATP酶的最适温度，这表明ATP酶的热稳定性取决于酶周围的磷脂。向蝗虫和小龙虾SR的脱脂ATP酶中添加二硬脂酰磷脂酰胆碱可提高热稳定性，而添加二亚油酰磷脂酰胆碱和二肉豆蔻酰磷脂酰胆碱时则会观察到热稳定性降低。这些结果表明，ATP酶的热稳定性可能受酶微环境中脂肪酰链构象的影响。
