The glycophorin-phospholipid interface in recombined systems. A 31P-nuclear magnetic resonance study.
Glycophorin, the MN glycoprotein from the erythrocyte membrane, was recombined with egg phosphatidylcholine and with the total lipid extract from human erythrocyte membranes in a membranous form. 31P-nuclear magnetic resonance (NMR) spectra of the recombinants resembled spectra obtained from unsonicated phospholipid dispersions and biological membranes. The glycophorin/phospholipid ratio in these recombinants was varied from approximately 50:1 (lipid/protein) to 200:1, and 31P-NMR spectral intensities were obtained. Comparison of these intensities to that expected based on a pure phospholipid standard revealed that there were two phospholipid environments in the recombinants: one immobilized by the protein, and one slightly disordered and nonimmobilized. A relatively constant number of phospholipids were immobilized per glycophorin at all lipid/protein ratios studied.
D002462:Cell Membrane; D055598:Chemical Phenomena; D002621:Chemistry; D006021:Glycophorins; D008051:Lipid Bilayers; D009682:Magnetic Resonance Spectroscopy; D008563:Membrane Lipids; D008954:Models, Biological; D010713:Phosphatidylcholines; D012795:Sialoglycoproteins
D006021:Glycophorins; D008051:Lipid Bilayers; D008563:Membrane Lipids; D010713:Phosphatidylcholines; D012795:Sialoglycoproteins