肌浆网中的脂-蛋白相互作用不受离子载体A23187的干扰。一项电子顺磁共振和荧光研究。
Lipid-protein interactions in sarcoplasmic reticulum are not perturbed by ionophore A23187. An EPR and fluorescence study.
作者信息
Pringle M J, Hidalgo C
出版信息
Biophys J. 1982 Mar;37(3):633-6.
Abstract
The divalent-cation ionophore A23187 at micromolar concentrations prevents the ATP-dependent accumulation of calcium into sarcoplasmic reticulum vesicles. Under the same conditions and throughout the temperature range of 4 degrees-37 degrees C, A23187 has no effect on either the rotational motion of the Ca2+ -ATPase in the membrane, or on the mobility of the lipid acyl chains. The steady-state fluorescence polarization of a polyene fluorescent probe incorporated into the membrane lipids was similarly unaffected by the ionophore. These results show conclusively that the mechanism of action of the ionophore does not involve significant of lipid-protein interactions.
摘要
微摩尔浓度的二价阳离子载体A23187可阻止ATP依赖的钙向肌浆网囊泡内积聚。在相同条件下以及4℃至37℃的整个温度范围内，A23187对膜中Ca2 + -ATP酶的旋转运动或脂质酰基链的流动性均无影响。掺入膜脂中的多烯荧光探针的稳态荧光偏振同样不受该离子载体的影响。这些结果确凿地表明，该离子载体的作用机制不涉及显著的脂-蛋白相互作用。
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