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. 1974 Dec;71(12):4653–4657. doi: 10.1073/pnas.71.12.4653

Glycophorin in Lipid Bilayers

Chris W M Grant 1,*, Harden M McConnell 1,†
PMCID: PMC433953  PMID: 4373724

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.

Keywords: lipid-protein interactions, freeze-fracture electron microscopy, spin labels, glycoproteins, lateral phase separations

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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