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PMID: 287077 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Syndeins: the spectrin-binding protein(s) of the human erythrocyte membrane.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 76 ·No. 5 ·1979-05-00 ·Pages 2340-4

Yu J, Goodman SR

Abstract

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.

MeSH Terms
Carrier Proteins/blood Erythrocyte Membrane/analysis Erythrocytes/analysis Humans Membrane Proteins/blood,metabolism Molecular Weight Peptide Fragments/analysis Spectrin/metabolism
Chemicals
Carrier Proteins Membrane Proteins Peptide Fragments Spectrin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Yu J
Goodman S R
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21 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.76.5.2340
Published
1979-05-00
Pages
2340-4
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC383596
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.76.5.2340 PMC Full Text View journal details
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