Brown R E, Cunningham C C
Biochim Biophys Acta. 1982 Jan 4;684(1):141-5. doi: 10.1016/0005-2736(82)90059-1.
The highly-purified, oligomycin-sensitive mitochondrial adenosine triphosphatase has been reconstituted with phosphatidylserine. Treatment of the phosphatidylserine-reconstituted ATPase with phosphatidylserine decarboxylase produced a 3-fold decrease in the specific activity of the resulting phosphatidylethanolamine-enriched ATpase complex. Subsequent control experiments indicated that the resulting phosphatidylethanolamine was responsible for the lowered ATPase specific activity. These observations indicate that acidic phospholips do more than facilitate and interaction between the highly-purified, lipid-depleted ATPase and phospholipid. The negatively charged phospholipid appears to be essential for maintaining high levels of oligomycin-sensitive activity even after the initial interaction between phospholipid and the ATPase complex has occurred.
高纯度的、对寡霉素敏感的线粒体腺苷三磷酸酶已用磷脂酰丝氨酸进行了重组。用磷脂酰丝氨酸脱羧酶处理磷脂酰丝氨酸重组的ATP酶，使所得富含磷脂酰乙醇胺的ATP酶复合物的比活性降低了3倍。随后的对照实验表明，所得的磷脂酰乙醇胺是ATP酶比活性降低的原因。这些观察结果表明，酸性磷脂的作用不仅仅是促进高度纯化的、脱脂的ATP酶与磷脂之间的相互作用。即使在磷脂与ATP酶复合物发生初始相互作用之后，带负电荷的磷脂似乎对于维持高水平的寡霉素敏感性活性也是必不可少的。
