Syndeins: the spectrin-binding protein(s) of the human erythrocyte membrane.
- 1 May 1979
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 76 (5) , 2340-2344
- https://doi.org/10.1073/pnas.76.5.2340
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.This publication has 20 references indexed in Scilit:
- Self‐Association of Human SpectrinEuropean Journal of Biochemistry, 1978
- Purification of an active proteolytic fragment of the membrane attachment site for human erythrocyte spectrin.Journal of Biological Chemistry, 1978
- Triton shells of intact erythrocytesJournal of Supramolecular Structure, 1978
- Spectrin binding and the control of membrane protein mobilityJournal of Supramolecular Structure, 1978
- Radioiodination of proteins in single polyacrylamide gel slices. Tryptic peptide analysis of all the major members of complex multicomponent systems using microgram quantities of total protein.Journal of Biological Chemistry, 1977
- On the mechanism of ATP-induced shape changes in the human erythrocyte membranes: the role of ATPThe Journal of cell biology, 1977
- Selective association of spectrin with the cytoplasmic surface of human erythrocyte plasma membranes. Quantitative determination with purified (32P)spectrin.Journal of Biological Chemistry, 1977
- Reconstitution of intramembrane particles in recombinants of erythrocyte protein band 3 and lipid: effects of spectrin-actin association.Proceedings of the National Academy of Sciences, 1976
- The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytesArchives of Biochemistry and Biophysics, 1963
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951