Hargreaves W R, Giedd K N, Verkleij A, Branton D
J Biol Chem. 1980 Dec 25;255(24):11965-72.
The binding of human erythrocyte ankyrin (band 2.1) to the erythrocyte membrane has been characterized by reassociating purified ankyrin with ankyrin-depleted inside-out vesicles. Ankyrin reassociates at high affinity with a limited number of protease-sensitive sites located only on the cytoplasmic side of the erythrocyte membrane. Depleting the vesicles of band 4.2 does not affect their binding capacity. A 45,000-dalton polypeptide derived from the cytoplasmic portion of band 3 competitively inhibits the binding of ankyrin to inside-out vesicles. Although the bulk of band 3 molecules appear to have the potential for binding ankyrin, nly a fraction of the band 3 molecules in native membranes or in reconstituted liposomes actually provides accessible high affinity ankyrin binding sites.
人红细胞锚蛋白（带2.1）与红细胞膜的结合已通过将纯化的锚蛋白与耗尽锚蛋白的内向外囊泡重新结合来进行表征。锚蛋白以高亲和力与仅位于红细胞膜细胞质侧的有限数量的蛋白酶敏感位点重新结合。耗尽带4.2的囊泡不影响其结合能力。源自带3细胞质部分的45,000道尔顿多肽竞争性抑制锚蛋白与内向外囊泡的结合。尽管大部分带3分子似乎具有结合锚蛋白的潜力，但天然膜或重组脂质体中只有一部分带3分子实际提供可及的高亲和力锚蛋白结合位点。
