Yu J, Goodman S R
Proc Natl Acad Sci U S A. 1979 May;76(5):2340-4. doi: 10.1073/pnas.76.5.2340.
Two-dimensional tryptic and chymotryptic analyses of all the major bands in a sodium dodecyl sulfate/polyacrylamide gel of the human erythrocyte membrane show that each band has a characteristic map. However, band 2.1 (nomenclature of T. L. Steck) and several polypeptides below this band exhibit similar tryptic and chymotryptic peptide maps and thus appear to be a family of closely related proteins or degradation products. Furthermore, they all contain a subset of peptides that are accounted for by the peptides from two known spectrin-binding fragments. We show that both fragments derive from 2.1-related proteins and conclude that band 2.1 and its related proteins, which we name "syndeins", bind spectrin and connect it to the erythrocyte membrane.
对人红细胞膜十二烷基硫酸钠/聚丙烯酰胺凝胶中所有主要条带进行二维胰蛋白酶和胰凝乳蛋白酶分析表明,每条带都有一个特征图谱。然而,带2.1(T. L. Steck的命名法)及其下方的几种多肽表现出相似的胰蛋白酶和胰凝乳蛋白酶肽图谱,因此似乎是一组密切相关的蛋白质或降解产物。此外,它们都包含一个肽子集,这些肽由来自两个已知血影蛋白结合片段的肽组成。我们表明这两个片段都来自与2.1相关的蛋白质,并得出结论,带2.1及其相关蛋白质,我们将其命名为“联蛋白”,结合血影蛋白并将其连接到红细胞膜上。