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Scandinavian Journal of Clinical and Laboratory Investigation Volume 38, 1978 - Issue sup150
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Original Article

Purification and Characterization of Lecithin:Cholesterol Acyltransferase

E. Gustow Lipid Research Laboratory, Dept. of Medicine, Temple University Health Sciences Center, Philadelphia, Pennsylvania, USA
,
K. G. Varma Lipid Research Laboratory, Dept. of Medicine, Temple University Health Sciences Center, Philadelphia, Pennsylvania, USA
&
L. A. Soloff Lipid Research Laboratory, Dept. of Medicine, Temple University Health Sciences Center, Philadelphia, Pennsylvania, USA
Pages 1-5 | Published online: 08 Jul 2009
 
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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.

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