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Science 22 November 1968:
Vol. 162. no. 3856, pp. 909 - 911
DOI: 10.1126/science.162.3856.909
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Articles

Structure of Human Serum Lipoproteins: Nuclear Magnetic Resonance Supports a Micellar Model

Joseph M. Steim 1, Orville J. Edner 1, and Frederick G. Bargoot 1

1 Chemistry Department, Brown University, Providence, Rhode Island 02912

High-resolution proton nuclear magnetic resonance spectra of low- and high-density lipoproteins from human serum closely resemble those of dispersions of lipoprotein lipids in water. Linewidths of hydrocarbon proton absorptions are not increased in the lipoproteins. In contrast, apolar binding of lysolecithin on serum albumin causes extensive line-broadening and an upfield chemical shift of the hydrocarbon proton resonances of lysolecithin. The results are consistent with a predominantly micellar structure for the lipoproteins rather than with extensive hydrophobic association of lipid and protein.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Natural Abundance Carbon-13 Nuclear Magnetic Resonance Spectra of Human Serum Lipoproteins.
J. A. Hamilton, C. Talkowski, E. Williams, E. M. Avila, A. Allerhand, E. H. Cordes, and G. Camejo (1973)
Science 180, 193-195
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Science. ISSN 0036-8075 (print), 1095-9203 (online)