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Journal of Lipid Research, Vol. 46, 1624-1632, August 2005
Copyright © 2005 by American Society for Biochemistry and Molecular Biology

* Department of Nutrition and Food Science, University of Maryland, College Park, MD 20742
Department of Poultry Science, Texas A&M University, College Station, TX 77843-2472
Published, JLR Papers in Press, June 1, 2005. DOI 10.1194/jlr.M400434-JLR200
1 To whom correspondence should be addressed. e-mail: eboyle-r{at}chemistry.ohio-state.edu
High-resolution NMR was used to measure the presence and quantity of triacylglycerol (TAG) in the surface of intact native apolipoprotein B-100-containing lipoprotein particles that are made by chickens in response to estrogen treatment and that in hens are deposited in yolk follicles (VLDLy). Integration of 13C NMR resonances shows that intact VLDLy particles contain more surface TAG (5.1 ± 0.6 mol%, 6.7 ± 0.8 weight %) than predicted by apolipoprotein-free models using similarly acyl-heterogenous TAG. Change in downfield chemical shift values of surface to core TAG in VLDLy was 0.8 ppm compared with 1.3 ppm in vesicles prepared with purified egg phosphatidylcholine and TAG isolated from the VLDLy, indicating that reduced surface TAG hydration may contribute to the resistance to lipase hydrolysis characteristic of this lipoprotein species.
Apolipoprotein-mediated changes in surface lipid composition and lipid hydration provide possible general mechanisms for selectivity in lipoprotein substrate characteristics.
Abbreviations: apoB-100, apolipoprotein B-100; CE, cholesteryl ester; DES, diethylstilbestrol; NOE, nuclear Overhauser enhancement; PC, phosphatidylcholine; PL, phospholipid; TAG, triacylglycerol; UC, unesterified cholesterol; VLDLy, yolk-deposited very low density lipoprotein
Supplementary key words apolipoprotein B-100 yolk-deposited very low density lipoproteins 13C nuclear magnetic resonance surface lipid estrogen birds
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