Patsch J R, Soutar A K, Morrisett J D, Gotto A M, Smith L C
Eur J Clin Invest. 1977 Jun;7(3):213-7. doi: 10.1111/j.1365-2362.1977.tb01600.x.
The action of lecithin:cholesterol acyltransferase (LCAT) was studied on an abnormal lipoprotein (LP-X) rich in phosphatidylcholine and cholesterol from the plasma of patients with obstructive liver disease. 60 mg LP-X isolated free of other lipoproteins and subsequently labelled with 3H-cholesterol were incubated with 1 mg highly purified enzyme in the presence of albumin. After 45 h at 37 degrees C, the incubation mixture was subjected to zonal ultracentrifugation. 3H-cholesterol and 3H-cholesteryl esters were quantified in each fraction of the zonal gradient. More than 95% of the lipoproteins in this mixture banded in the density range of LP-X with no change in size distribution, but did contain 593 nmoles of newly formed cholesteryl esters. Agarose electrophoresis revealed an alpha-migrating band in addition to the original beta-band. Also on agar, the typically cathode migrating LP-X was changed to anode moving material. These studies indicate that LP-X can serve as a substrate for LCAT.
对阻塞性肝病患者血浆中富含磷脂酰胆碱和胆固醇的异常脂蛋白（LP-X）进行了卵磷脂：胆固醇酰基转移酶（LCAT）的作用研究。将60mg不含其他脂蛋白并随后用3H-胆固醇标记的LP-X与1mg高度纯化的酶在白蛋白存在下孵育。在37℃下孵育45小时后，将孵育混合物进行区带超速离心。在区带梯度的每个级分中对3H-胆固醇和3H-胆固醇酯进行定量。该混合物中超过95%的脂蛋白在LP-X的密度范围内形成条带，大小分布没有变化，但确实含有593纳摩尔新形成的胆固醇酯。琼脂糖电泳显示除了原来的β带外还有一个α迁移带。同样在琼脂上，典型的向阴极迁移的LP-X变成了向阳极移动的物质。这些研究表明LP-X可以作为LCAT的底物。
