title: Phosphatidylcholine substrate specificity of lecithin:cholesterol acyltransferase.
abstract: 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.
mesh_terms: D055598:Chemical Phenomena; D002621:Chemistry; D002788:Cholesterol Esters / Q000032:analysis; D005227:Fatty Acids / Q000032:analysis; D006801:Humans; D008968:Molecular Conformation; D007862:Phosphatidylcholine-Sterol O-Acyltransferase / Q000032:analysis / Q000302:isolation & purification; D010713:Phosphatidylcholines / Q000032:analysis / Q000138:chemical synthesis*
chemical_list: D002788:Cholesterol Esters; D005227:Fatty Acids; D010713:Phosphatidylcholines; D007862:Phosphatidylcholine-Sterol O-Acyltransferase