31P nuclear magnetic resonance evidence for polyphosphoinositide associated with the hydrophobic segment of glycophorin A.
Glycophorin A, the major human erythrocyte sialoglycoprotein, contains a significant amount of phosphorus when isolated by the lithium diiodosalicylate-phenol procedure. Only a small percentage (approximately 1%) of this phosphorus is phosphoprotein. 31P nuclear magnetic resonance (NMR) analysis of glycophorin A has identified the remaining phosphorus content as phospholipid in origin. From the 31P chemical shifts, the phospholipid has been identified as diphosphoinositide. 31P NMR spectra of the peptides produced by trypsin hydrolysis of glycophorin A reveal that all the diphosphoinositide is closely associated with the hydrophobic region of the protein, suggesting that there is a specific affinity between this phospholipid and the intramembranous portion of glycophorin A.
D001665:Binding Sites; D004910:Erythrocyte Membrane; D006021:Glycophorins; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D010446:Peptide Fragments / Q000032:analysis; D010716:Phosphatidylinositols / Q000097:blood*; D011485:Protein Binding; D011487:Protein Conformation; D012795:Sialoglycoproteins; D014357:Trypsin
D006021:Glycophorins; D010446:Peptide Fragments; D010716:Phosphatidylinositols; D012795:Sialoglycoproteins; D014357:Trypsin