Proton NMR studies of vesicles incorporating glycophorin.
The effects of incorporation of glycophorin, the major sialoglycoprotein of the human erythrocyte membrane, on the lipid of small vesicles have been studied using proton NMR and electron microscopy. In contrast to the incorporation of other peptides, the major effect is apparently the clustering of vesicles without fusion. The relative mobility of lipids of the vesicle, monitored by changes in proton spin-lattice time, is only moderately effected by the presence of protein. The methylene protons of the lipid chains are subject to a somewhat greater restriction of motion following the incorporation of glycophorin than are the protons of the head group.
D000596:Amino Acids / Q000032:analysis; D004910:Erythrocyte Membrane / Q000032:analysis; D006021:Glycophorins / Q000302:isolation & purification; D006801:Humans; D008081:Liposomes; D009682:Magnetic Resonance Spectroscopy; D008854:Microscopy, Electron; D008970:Molecular Weight; D011663:Pulmonary Surfactants; D012795:Sialoglycoproteins / Q000302:isolation & purification
D000596:Amino Acids; D006021:Glycophorins; D008081:Liposomes; D011663:Pulmonary Surfactants; D012795:Sialoglycoproteins