Assmann G, Schmitz G, Donath N, Lekim D
Scand J Clin Lab Invest Suppl. 1978;150:16-20.
Lecithin:cholesterol acyltransferase (LCAT) has been partially purified by the combined method of ultracentrifugation and dextranblue-2000 4 B affinity chromatography. The enzyme was incubated with liposomes consisting of phosphatidylcholine-cholesterol in a molar ratio of 10/1. Chemically synthesized phosphatidylcholine substrates with labeled fatty acids in 1-and 2-position were chosen to evaluate the degree of transesterification. It was found that the fatty acid in the 1-position of phosphatidylcholine significantly influences cholesteryl ester formation, both by its direct involvement in the LCAT reaction and its contribution to the physico-chemical properties of phosphatidylcholine.
卵磷脂胆固醇酰基转移酶（LCAT）已通过超速离心和葡聚糖蓝-2000 4B亲和色谱联合法进行了部分纯化。该酶与摩尔比为10/1的磷脂酰胆碱-胆固醇组成的脂质体一起孵育。选择在1位和2位带有标记脂肪酸的化学合成磷脂酰胆碱底物来评估酯交换程度。结果发现，磷脂酰胆碱1位的脂肪酸通过其直接参与LCAT反应及其对磷脂酰胆碱物理化学性质的贡献，对胆固醇酯的形成有显著影响。
