Isern de Caldentey M, Wheeler K P
Biochem J. 1979 Jan 1;177(1):265-73. doi: 10.1042/bj1770265.
The basis of the requirement for a net negative charge on phospholipid dispersions able to re-activate lipid-depleted (Na++K+)-dependent adenosine triphosphatase was studied. The origin and density of the charge in phospholipid dispersions were varied before interaction with the adenosine triphosphatase protein, and the charge density on restored phospholipid-adenosine triphosphatase complexes was changed after interaction. The results indicated that: (a) re-activation requires a lamellar arrangement of the lipid molecules with sufficient density of negative charge, but not necessarily negatively charged phospholipid molecules; (b) the net charge appears to be necessary for the correct interaction between the enzyme protein and the phospholipids, although the amount of phospholipid that binds to the protein is also a function of the nature of the acyl chains; (c) it is not possible on the basis of these findings and those in the literature to decide unequivocally if the charge is also required for the enzyme reaction itself. The possible relevance of the findings to the situation in vivo is discussed in terms of the charge being concerned only with lipid-protein interaction.
对能够重新激活脂质耗尽的（Na++K+）依赖性三磷酸腺苷酶的磷脂分散体上净负电荷要求的基础进行了研究。在与三磷酸腺苷酶蛋白相互作用之前，改变磷脂分散体中电荷的来源和密度，并在相互作用后改变恢复的磷脂 - 三磷酸腺苷酶复合物上的电荷密度。结果表明：（a）重新激活需要脂质分子呈层状排列且具有足够的负电荷密度，但不一定需要带负电荷的磷脂分子；（b）净电荷似乎是酶蛋白与磷脂之间正确相互作用所必需的，尽管与蛋白结合的磷脂量也是酰基链性质的函数；（c）基于这些发现和文献中的发现，无法明确确定该电荷对于酶反应本身是否也是必需的。就该电荷仅与脂质 - 蛋白质相互作用有关而言，讨论了这些发现与体内情况的可能相关性。
