Abstract
Two-dimensional tryptic and chymotryptic analyses of all the major bands in a sodium dodecyl sulfate/polyacrylamide gel of the human erythrocyte membrane showed that each band has a characteristic map. Band 2.1 (nomenclature of T. L. Steck) and several polypeptides below this band exhibited similar tryptic and chymotryptic peptide maps and thus appeared to be a family of closely related proteins or degradation products. They all contained a subset of peptides that were accounted for by the peptides from 2 known spectrin-binding fragments. Both fragments derived from 2.1-related proteins. Band 2.1 and its related proteins, named syndeins, bind spectrin and connect it to the erythrocyte membrane.