Phosphorus nuclear magnetic resonance studies of lipid-protein interactions: human erythrocyte glycophorin and phospholipids.
Human erythrocyte glycophorin containing four molecules of phospholipid tightly bound to the protein was isolated from human red cell ghosts. This protein preparation was reconstituted into a digalactosyl diglyceride bilayer. The 31P NMR spectrum of this reconstituted membrane produced an axially symmetric powder pattern arising exclusively from the phospholipids bound to glycophorin. The width of the powder pattern, about 90 ppm, is about twice as broad as that normally exhibited by a phospholipid bilayer. The chemical shift tensor is perturbed relative to phospholipids in a bilayer. The spin-lattice relaxation rate of these protein-bound phospholipids is found to be nearly an order of magnitude faster than phospholipids in a bilayer. The results are consistent with phospholipids tightly bound to the membrane protein and undergoing rotational diffusion, perhaps as a complex of phospholipid and protein.
Yeagle
P L
PL
Department of Biochemistry, University at Buffalo School of Medicine (SUNY) 14214.
Kelsey
D
D
D004910:Erythrocyte Membrane / Q000378:metabolism*; D006021:Glycophorins / Q000378:metabolism*; D006801:Humans; D008051:Lipid Bilayers / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D010743:Phospholipids / Q000097:blood*; D011485:Protein Binding; D011487:Protein Conformation; D012795:Sialoglycoproteins / Q000378:metabolism*
D006021:Glycophorins; D008051:Lipid Bilayers; D010743:Phospholipids; D012795:Sialoglycoproteins