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PMID: 4373724 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

Glycophorin in lipid bilayers.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 71 ·No. 12 ·1974-12-00 ·Pages 4653-7

Grant CW, McConnell HM

Abstract

Glycophorin, the major glycoprotein of human erythrocytes, has been isolated and reincorporated into lipid vesicles. Freeze-fracture electron microscopy shows the reincorporated glycophorin to occur as small particles in vesicle fracture faces while the etch faces are smooth. The glycoprotein has a tendency to cluster into groups of several particles. Evidence is presented that, although lipids in immediate contact with glycopherin are likely somewhat immobilized, the entire lipid-protein complex has a tendency to occupy fluid regions of the bilayer. Reincorporated glycophorin assumes its proposed conformation in the intact erythrocyte in so far as it penetrates the hydrophobic membrane interior while its N-terminal end with attached carbohydrate residues is exposed to the aqueous compartment and is available as a specific recognition site.

MeSH Terms
Cell Membrane/analysis Electron Spin Resonance Spectroscopy Erythrocytes/analysis Freeze Etching Glycoproteins/isolation & purification Humans Lipids Membranes, Artificial Microscopy, Electron Protein Conformation Spin Labels
Chemicals
Glycoproteins Lipids Membranes, Artificial Spin Labels
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Grant C W
McConnell H M
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32 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.71.12.4653
Published
1974-12-00
Pages
4653-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC433953
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.71.12.4653 PMC Full Text View journal details
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