Nuclear magnetic resonance studies of rat serum lipoproteins

✍ Scribed by N.H. Fidge; I.C. Calder

• Publisher: Elsevier Science
• Year: 1972
• Tongue: English
• Weight: 393 KB
• Volume: 9
• Category: Article
• ISSN: 0009-3084
• DOI: 10.1016/0009-3084(72)90013-8

✦ Synopsis

The structure of rat lipoproteins was investigated by comparing the Nuclear Magnetic Resonance (NMR) spectra of four serum lipoproteins of different lipid: protein ratios. Signals associated with the lipid moieties were prominent and well resolved in the spectrum of each lipoprotein and a clear trend was observed in the relative areas of some peaks, notably in the (CH2)n:CHa area ratios which correlated well with the chemical composition of the macromolecules.

In all cases, raising the temperature caused an increased sharpness of the major peaks (-CHa, (CH2)n and N+(CHa)a) while alteration of the pH from 2.5 to 11.0 had little effect on the spectra of all four lipoproteins. Studies on partially delipidated rat high density lipoprotein (HDL) and reconstituted HDL indicated that altering the amount of phospholipid in the protein-phospholipid complex considerably influenced its structure, resulting in more compactly organized complexes at higher phospholipid:protein ratios than at lower ratios.