Nöthig-Laslo V, Jürgens G, Holasek A
Chem Phys Lipids. 1984 Jul;35(2):143-50. doi: 10.1016/0009-3084(84)90020-3.
The effect of Ca2+ binding on the dynamic properties of various spin labeled fatty acids in lipoprotein(a) (Lp(a)) was studied in comparison with low density lipoprotein (LDL) isolated from human plasma. In contrast to LDL, binding of Ca2+ to Lp(a) induced broadening of the lines in the ESR spectra of the spin labeled stearic acids. In 1.6 M NaBr solutions the thermotropic change in the surface structure was observed in both lipoproteins at similar temperatures. Ten millimolar concentration of Ca2+ shifted the temperature of the thermotropic change in the surface structure of Lp(a) to considerably higher values. We conclude that Ca2+ binding to Lp(a) induces changes in the lipid structure of the particle surface.
与从人血浆中分离出的低密度脂蛋白（LDL）相比，研究了Ca2+结合对脂蛋白(a)（Lp(a)）中各种自旋标记脂肪酸动态特性的影响。与LDL不同，Ca2+与Lp(a)的结合导致自旋标记硬脂酸的电子自旋共振（ESR）光谱中的谱线变宽。在1.6 M NaBr溶液中，在相似温度下两种脂蛋白均观察到表面结构的热致变化。10 mM浓度的Ca2+将Lp(a)表面结构热致变化的温度显著提高。我们得出结论，Ca2+与Lp(a)的结合会引起颗粒表面脂质结构的变化。
