Purification and Characterization of Lecithin:Cholesterol Acyltransferase

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 elec...

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Veröffentlicht in:	Scandinavian journal of clinical & laboratory investigation. Supplement 1978, Vol.38 (S150), p.1-5
Hauptverfasser:	Gustow, E., Varma, K. G., Soloff, L. A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acids - analysis Carbohydrates - analysis Chromatography Electrophoresis, Polyacrylamide Gel enzyme Humans Hydroxyapatites hydroxylapatite Immunodiffusion Isoelectric Focusing Phosphatidylcholine-Sterol O-Acyltransferase - analysis Phosphatidylcholine-Sterol O-Acyltransferase - blood Phosphatidylcholine-Sterol O-Acyltransferase - isolation & purification plasma Urea - analysis
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Zusammenfassung:	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.
ISSN:	0036-5513 0085-591X 1502-7686
DOI:	10.3109/00365517809104891