Mikkelsen A, Stokke B T, Elgsaeter A
Biochim Biophys Acta. 1984 Apr 27;786(1-2):95-102. doi: 10.1016/0167-4838(84)90158-4.
In order to determine whether the presence of Ca2+ increases the stiffness of the highly elongated and flexible spectrin molecules, we have carried out a birefringence relaxation study of isolated human erythrocyte spectrin dimers. Our measurements indicate no significant change in the flexibility of spectrin in solutions containing 0-10(-3) M Ca2+. This finding indicates that decreased spectrin flexibility is not the major functional mechanism underlying the decreased erythrocyte deformability reported as result of elevated intracellular levels of Ca2+. We find that the persistence length of spectrin dimers is less than 20 nm and is not dependent on the Ca2+ concentration.
为了确定钙离子的存在是否会增加高度细长且柔韧的血影蛋白分子的刚性,我们对分离出的人红细胞血影蛋白二聚体进行了双折射弛豫研究。我们的测量结果表明,在含有0至10⁻³ M钙离子的溶液中,血影蛋白的柔韧性没有显著变化。这一发现表明,血影蛋白柔韧性降低并非细胞内钙离子水平升高导致红细胞变形性降低的主要功能机制。我们发现血影蛋白二聚体的持久长度小于20纳米,且不依赖于钙离子浓度。