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PMID: 723278 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Spectrin binding and the control of membrane protein mobility.

Journal of supramolecular structure ·Vol. 8 ·No. 4 ·1978-00-00 ·Pages 455-63

Goodman SR, Branton D

Abstract

Transmembrane proteins of the human erythrocyte show restricted in-plane mobility. Many of the restrictions on mobility are attributable to the molecules of spectrin which are located on the protoplasmic surface of the erythrocyte membrane. These molecules are elongate, form end-to-end heterodimer associations, and bind selectively to protein (or proteins) accessible on inside-out, but not right-side out, membrane vesicles.

MeSH Terms
Actins/blood Erythrocyte Membrane/physiology,ultrastructure Erythrocytes/physiology Membrane Fluidity Membrane Proteins/blood,metabolism Molecular Weight Protein Binding Spectrin/metabolism
Chemicals
Actins Membrane Proteins Spectrin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Goodman S R
Branton D
Article Info
Journal
Journal of supramolecular structure
Abbr.
J Supramol Struct
ISSN
0091-7419
Published
1978-00-00
Pages
455-63
Language
English
Region
United States
NLM ID
0330464
Subset
IM
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