Páli T, Ebert B, Horváth L I
Institute of Biophysics, Biological Research Center, Szeged, Hungary.
Biochim Biophys Acta. 1987 Nov 13;904(2):346-52. doi: 10.1016/0005-2736(87)90384-1.
Using a modulated magnetic field gradient technique, the conventional ESR spectrum of well-defined spatial sections and the one-dimensional-ESR image of the nitroxide centre line of spin-labeled stearic acid in phospholipid vesicles were recorded with a spatial resolution of 4.10(-5) m after pelleting the vesicles inside 1 mm (i.d.) sample capillaries in a slow centrifuge (2500 X g). The sedimentation characteristics of dimyristoylphosphatidylcholine and dimyristoylphosphatidylglycerol vesicles were quantitatively compared with particular reference to vesicle aggregation induced by myelin basic protein. Protein-induced changes in the effective molecular mass were determined from ESR images of sedimentation profiles. The present data lend further support to the notion that the primary target of myelin basic protein-lipid interaction is the acidic lipid pool of myelin.
采用调制磁场梯度技术，在将磷脂囊泡置于内径为1mm的样品毛细管中，通过低速离心机（2500×g）沉淀后，以4×10⁻⁵m的空间分辨率记录了磷脂囊泡中自旋标记硬脂酸氮氧化物中心线的明确空间截面的常规电子自旋共振（ESR）光谱和一维ESR图像。特别参照髓鞘碱性蛋白诱导的囊泡聚集，对二肉豆蔻酰磷脂酰胆碱和二肉豆蔻酰磷脂酰甘油囊泡的沉降特性进行了定量比较。从沉降曲线的ESR图像确定了蛋白质诱导的有效分子量变化。目前的数据进一步支持了髓鞘碱性蛋白 - 脂质相互作用的主要靶点是髓鞘酸性脂质池这一观点。
