Phosphatidylcholine substrate specificity of lecithin:cholesterol acyltransferase.
Phosphatidylcholine substrate specificity of lecithin:cholesterol acyltransferase.
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卵磷脂的磷脂酰胆碱底物特异性：胆固醇酰基转移酶。
DOI：
10.1080/00365517809104894
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发表时间：
1978
期刊：
影响因子：
--
通讯作者：
D. Lekim
中科院分区：
文献类型：
--
作者：
G. Assmann;G. Schmitz;N. Donáth;D. Lekim
卵磷脂：胆固醇酰基转移酶（LCAT）已通过超速离心和 dextranblue-2000 4 B 亲和层析相结合的方法进行部分纯化。该酶与由摩尔比为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。研究发现，磷脂酰胆碱 1 位的脂肪酸通过直接参与 LCAT 反应以及对磷脂酰胆碱的物理化学性质的贡献，显着影响胆固醇酯的形成。
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.