The Use of Paramagnetic Probes in the Structure Determination of High Density Serum Lipoproteins
The subject of this paper is the structure of high density lipoproteins (HDL) with particular reference to the nature of the lipid — protein interaction. The question of whether or not there are any general principles underlying the lipid — protein interaction in serum lipoproteins is of prime importance and will be discussed here. The work to be described was carried out with the HDL3 fraction isolated from porcine plasma and characterized by an operationally defined density of 1.12–1.21 g/ml. Results obtained with the native system will be compared with those of a model system reconstituted from lecithin and apoproteins isolated from porcine HDL3 lipoprotein. Several papers have discussed the striking compositional and structural similarities of human and porcine lipoproteins (1–4), and it is believed that the principles governing the lipid — protein interaction are generally applicable. To support this some experiments were repeated with human HDL of an operationally defined density d = 1.063–1.21 g/ml. The physical techniques used to derive the structural information to be discussed here are mainly NMR and ESR spectroscopy. Because of the small size of the high density lipoprotein particles (see below) the tumbling rate is sufficiently fast as to average out any residual dipolar broadening of NMR lines. Hence good high resolution spectra are obtained from high density lipoproteins.
KeywordsHigh Density Lipoprotein Cholesteryl Ester High Density Lipoprotein Paramagnetic Probe Relaxation Probe
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- (1).Davis, M.A.F., Henry, R. and Leslie, R.B. (1974) Comp. Biochem. Physiol., Vol. 47 B, pp 831–849.Google Scholar
- (2).Jackson, R.L., Baker, H.N., Taunton, O.D., Smith, L.C., Garner, C.W. and Gotto, A.M. (1973) J. Biol. Chem. 248, 2639–2644.Google Scholar
- (3).Mills, G.L. and Taylaur, C.E. (1971) Comp. Bio- chem. Physiol. 40 B, 289–301.Google Scholar
- (4).Fidge, N. (1973) Biochim. Biophys. Acta 295, 258273.Google Scholar
- (5).Atkinson, D., Davis, M.A.F. and Leslie, R.B. (1974) Proc. R. Soc. Lond. B 186, 165–180.Google Scholar
- (9).Morrisett, J.D., Jackson, R.L. and Gotto, A.M., Jr. (1975) Ann. Rev. Biochem. 44, 183–207.Google Scholar
- (11).Finer, E.G., Henry, R., Leslie, R.B. and Robertson, R.N. (1975) Biochim. Biophys. Acta 380, 320–337.Google Scholar
- (12).Hubbel, W.L. and McConnell, H.M. (1971) J. Amer. Chem. Soc. 93, 314–326.Google Scholar
- (13).Davis, M.A.F., Hauser, H., Leslie, R.B. and Phillips, M.C. (1973) Biochim. Biophys. Acta 317, 214–218.Google Scholar
- (14).Hamilton, J.A., Talkowski, C., Childers, R.F., Williams, E., Allerhand, A. and Cordes, E.H. (1974) J. Biol. Chem. 249, 4872–4878.Google Scholar