Marcel Y L, Vézina C, Emond D, Verdery R B, Milne R W
J Lipid Res. 1981 Nov;22(8):1198-205.
Normal human plasma HDL was applied to a column of heparin-Sepharose in the presence of MnCl(2) and three fractions were obtained by stepwise elution with increasing NaCl concentrations: a non-retained fraction (NR, 78% of protein) and two retained fractions (R(1) and R(2), 18 and 2.5% of protein, respectively). Both unesterified and esterified cholesterol increased from NR to R(1) to R(2) but the increment was more pronounced for unesterified cholesterol. ApoA-II to apoA-I ratio was-lower in R(1) compared to NR but R(1) contained more apoC than NR. ApoE increased from NR to R(1) to R(2) (0.07, 0.4, and 14% of protein in each fraction, respectively) while apoB was found only in R(2). Agarose gel electrophoresis and immunoadsorbers for apoB and apoE showed that R(2) consisted of two major lipoprotein populations, one containing apoB and some apoE and the other containing apoE and no apoB. Cholesteryl ester transfer between each HDL subfraction and VLDL in the presence of partially purified cholesterol ester transfer protein was studied. NR and R(1) gave the highest initial rates of transfer for labeled cholesteryl ester which were corroborated by significant mass transfer of cholesteryl esters. From these results, we concluded that there is no connection between cholesteryl ester transfer and apoE. On the other hand, transfer from R(2) to VLDL followed different kinetics with a high zero hour transfer but with subsequently lower rates when compared to NR and R(1). The cholesteryl ester transfer activity in R(2) was mainly due to the presence of apoE-containing lipoproteins whereas those containing apoB had minimal transfer activity. However, because this transfer of label was not translated into significant mass transfer of cholesteryl ester to VLDL, the apoE-containing lipoproteins appear involved mainly in the equilibration of cholesteryl esters.-Marcel, Y. L., C. Vézina, D. Emond, R. B. Verdery, and R. W. Milne. High density lipoprotein subfractions isolated by heparin-Sepharose affinity chromatography and their role in cholesteryl ester transfer to very low density lipoproteins.
将正常人血浆高密度脂蛋白（HDL）在氯化锰（MnCl₂）存在的情况下应用于肝素 - 琼脂糖柱，并通过逐步增加氯化钠浓度进行洗脱，得到三个组分：一个未保留组分（NR，占蛋白质的78%）和两个保留组分（R₁和R₂，分别占蛋白质的18%和2.5%）。游离胆固醇和胆固醇酯均从NR到R₁再到R₂逐渐增加，但游离胆固醇的增加更为明显。与NR相比，R₁中载脂蛋白A-II与载脂蛋白A-I的比值较低，但R₁中的载脂蛋白C比NR更多。载脂蛋白E从NR到R₁再到R₂逐渐增加（各组分中分别占蛋白质的0.07%、0.4%和14%），而载脂蛋白B仅在R₂中被发现。琼脂糖凝胶电泳以及针对载脂蛋白B和载脂蛋白E的免疫吸附剂显示，R₂由两个主要的脂蛋白群体组成，一个含有载脂蛋白B和一些载脂蛋白E，另一个含有载脂蛋白E且不含载脂蛋白B。研究了在部分纯化的胆固醇酯转移蛋白存在的情况下，每个HDL亚组分与极低密度脂蛋白（VLDL）之间的胆固醇酯转移。NR和R₁对标记胆固醇酯的初始转移速率最高，胆固醇酯的大量转移证实了这一点。从这些结果我们得出结论，胆固醇酯转移与载脂蛋白E之间没有关联。另一方面，从R₂到VLDL的转移遵循不同的动力学，零时转移率很高，但与NR和R₁相比，随后的转移率较低。R₂中的胆固醇酯转移活性主要归因于含载脂蛋白E的脂蛋白的存在，而含载脂蛋白B的脂蛋白转移活性最小。然而，由于这种标记的转移并未转化为胆固醇酯向VLDL的大量转移，含载脂蛋白E的脂蛋白似乎主要参与胆固醇酯的平衡。——马塞尔，Y. L.，C. 韦齐纳，D. 埃蒙德，R. B. 韦德里，和R. W. 米尔恩。通过肝素 - 琼脂糖亲和色谱法分离的高密度脂蛋白亚组分及其在胆固醇酯向极低密度脂蛋白转移中的作用
