title: Glycophorin in lipid bilayers.
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: D002462:Cell Membrane / Q000032:analysis; D004578:Electron Spin Resonance Spectroscopy; D004912:Erythrocytes / Q000032:analysis; D005613:Freeze Etching; D006023:Glycoproteins / Q000302:isolation & purification; D006801:Humans; D008055:Lipids; D008567:Membranes, Artificial; D008854:Microscopy, Electron; D011487:Protein Conformation; D013113:Spin Labels
chemical_list: D006023:Glycoproteins; D008055:Lipids; D008567:Membranes, Artificial; D013113:Spin Labels