title: Purification and characterization of lecithin:cholesterol acyltransferase.
abstract: The purification of lecithin:cholesterol acyltransferase (LCAT] from human plasma is reported. Hydroxylapatite fractions were approximately 16,000 fold purified over the starting plasma and were free of high-density lipoprotein (HDL) and albumin. The enzyme showed one band on polyacrylamide gel electrophoresis, SDS-urea polyacrylamide gel electrophoresis, isoelectric focusing, and one arc in immunodiffusion against a goat antiserum preparation. It was determined to be a glycoprotein with a molecular weight of approximately 70,000 and a pI of 3.7--4.0.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D002241:Carbohydrates / Q000032:analysis; D002845:Chromatography; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D006882:Hydroxyapatites; D005779:Immunodiffusion; D007525:Isoelectric Focusing; D007862:Phosphatidylcholine-Sterol O-Acyltransferase / Q000032:analysis / Q000097:blood / Q000302:isolation & purification*; D014508:Urea / Q000032:analysis
chemical_list: D000596:Amino Acids; D002241:Carbohydrates; D006882:Hydroxyapatites; D014508:Urea; D007862:Phosphatidylcholine-Sterol O-Acyltransferase