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. Author manuscript; available in PMC: 2020 Jul 1.
Published in final edited form as: Biochim Biophys Acta Mol Cell Biol Lipids. 2019 Mar 5;1864(7):1061–1071. doi: 10.1016/j.bbalip.2019.03.001

Figure 3.

Figure 3.

Effects of endogenous TG levels on the lipoprotein remodeling and fusion. Single-donor VLDL and LDL with naturally occurring high and low TG were same as those in Figure 2. To compare the extent of thermal remodeling, the lipoproteins were incubated for 10 min at 85 °C followed by cooling to 25 °C and analysis by SEC using Superose 6 10/300 GL column (A, C), non-denaturing PAGE, 4% (B, D), and transmission electron microscopy (E) as described in part 2.3 Methods. Intact (unheated) lipoproteins were used as controls; SEC profiles for high-TG and low-TG controls fully superimposed. In panels A and B, exchangeable proteins released from VLDL are indicated; these proteins have been identified by mass spectrometry (Figure S3). In panels D and E, numbers mark intact-size LDL (1), fused LDL (2), and ruptured/aggregated LDL (3). White lines between the lanes indicate split gels (panel E and other gels throughout this paper).