Barnes G, Frieden E
Biochem Biophys Res Commun. 1984 Nov 30;125(1):157-62. doi: 10.1016/s0006-291x(84)80348-4.
Mammalian erythrocytes have been shown to bind 125I labeled ceruloplasmin. Binding was reversible and specific. Scatchard analysis yielded linear plots with a Kd of approximately 5nM. The binding site appeared to be a protein located on the cell surface. A ceruloplasmin binding protein with a molecular weight of 60,000 daltons was isolated from human erythrocytes. Erythrocytes which were not protected by ceruloplasmin's antioxidant properties, did not bind ceruloplasmin. Our results provide evidence for the presence of ceruloplasmin receptors in the erythrocyte membrane. It is proposed that the antioxidant activity of ceruloplasmin may play a role in determining the lifespan of circulating red cells.
哺乳动物红细胞已被证明能结合125I标记的铜蓝蛋白。结合是可逆且特异的。Scatchard分析得到线性图，解离常数（Kd）约为5nM。结合位点似乎是位于细胞表面的一种蛋白质。从人红细胞中分离出一种分子量为60,000道尔顿的铜蓝蛋白结合蛋白。未受铜蓝蛋白抗氧化特性保护的红细胞不结合铜蓝蛋白。我们的结果为红细胞膜中存在铜蓝蛋白受体提供了证据。有人提出，铜蓝蛋白的抗氧化活性可能在决定循环红细胞的寿命中起作用。
