Newton C, Pangborn W, Nir S, Papahadjopoulos D
Biochim Biophys Acta. 1978 Jan 19;506(2):281-7. doi: 10.1016/0005-2736(78)90398-x.
Differences in the interaction of Ca2+ and Mg2+ with phosphatidylserine vesicles were revealed by binding studies, differential scanning calorimetry and X-ray diffraction. The two cations produced structurally different complexes with phosphatidylserine as evidenced by phase transition characteristics, lamellar spacings, and hydrocarbon packing. Ca2+ effectively completes with Mg2+ for phosphatidylserine binding sites. Analysis of the binding data showed that Ca2+ had a ten-fold greater intrinsic binding constant for phosphatidylserine.
通过结合研究、差示扫描量热法和X射线衍射揭示了Ca2+和Mg2+与磷脂酰丝氨酸囊泡相互作用的差异。这两种阳离子与磷脂酰丝氨酸形成结构不同的复合物,这一点从相变特征、层间距和烃类堆积情况得到证明。Ca2+与Mg2+在磷脂酰丝氨酸结合位点上存在有效竞争。结合数据的分析表明,Ca2+对磷脂酰丝氨酸的内在结合常数大十倍。