Phospholipid-protein interactions in human low density lipoprotein detected by 31P nuclear magnetic resonance.
31P nuclear magnetic resonance (NMR) spectra of human low density lipoprotein (LDL) has been obtained and the major phospholipid components identified. Analysis of the spectra revealed two phospholipid environments: one occupied by 4/5 of the phospholipid with high resolution resonances possessing properties similar to phospholipids in vesicles, and a second occupied by 1/5 of the phospholipid with broad lines indicative of immobilization. Limited trypsin treatment of the particle cleaved all of the B peptide into smaller molecular weight peptides which remained with the particle. Trypsin-treated LDL eluted from a Sepharose CL-6B column similarly to native LDL so that the modified particle remained intact. 31P NMR spectra of trypsin-treated LDL showed little or no immobilized phospholipid. The immobilization in the native LDL particle is attributed to lipid-protein interactions between 1/5 of the phospholipid and the B peptide.
D001053:Apolipoproteins / Q000097:blood; D006801:Humans; D007122:Immunoelectrophoresis; D008077:Lipoproteins, LDL / Q000097:blood; D009682:Magnetic Resonance Spectroscopy; D010446:Peptide Fragments / Q000032:analysis; D010743:Phospholipids / Q000097:blood; D011485:Protein Binding; D011487:Protein Conformation; D014357:Trypsin
D001053:Apolipoproteins; D008077:Lipoproteins, LDL; D010446:Peptide Fragments; D010743:Phospholipids; D014357:Trypsin