Syndeins

The spectrin-binding protein(s) of the human erythrocyte membrane

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88 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)2340-2344
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume76
Issue number5
DOIs
StatePublished - Jan 1 1979

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Erythrocyte Membrane
Spectrin
Peptides
Terminology
Sodium Dodecyl Sulfate
Proteolysis
Names
Proteins
spectrin-binding proteins

All Science Journal Classification (ASJC) codes

  • General

Cite this

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title = "Syndeins: The spectrin-binding protein(s) of the human erythrocyte membrane",
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.",
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AU - Yu, J.

AU - Goodman, Steven

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N2 - 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.

AB - 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.

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