Characterization of lecithin:cholesterol acyltransferase from human plasma: Purification of the enzyme

Kui Song Chong, Leo Davidson, R. G. Huttash, Andras G. Lacko

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Lecithin:cholesterol acyltransferase was isolated from a human plasma fraction in a homogeneous state by an efficient and highly reproducible procedure. The purification scheme involved: (1) hydrophobic affinity chromatography, (2) DEAE-agarose chromatography, (3) delipidation, (4) a second DEAE-agarose chromatography, and (5) a combination of hydroxylapatite and antibody adsorption chromatography. The final product was purified 20,000-fold over the starting material and was found to be free of any polypeptide contaminant as indicated by gel electrophoresis, sedimentation equilibrium ultracentrifugation, immunodiffusion, and immunoelectrophoresis.

Original languageEnglish
Pages (from-to)119-124
Number of pages6
JournalArchives of Biochemistry and Biophysics
Volume211
Issue number1
DOIs
StatePublished - 1 Oct 1981

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Plasma (human)
Phosphatidylcholine-Sterol O-Acyltransferase
Agarose Chromatography
Chromatography
Purification
Sepharose
Immunoelectrophoresis
Hydrophobic chromatography
Immunodiffusion
Ultracentrifugation
Enzymes
Durapatite
Affinity Chromatography
Adsorption
Affinity chromatography
Electrophoresis
Gels
Sedimentation
Peptides
Antibodies

Cite this

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Characterization of lecithin:cholesterol acyltransferase from human plasma : Purification of the enzyme. / Chong, Kui Song; Davidson, Leo; Huttash, R. G.; Lacko, Andras G.

In: Archives of Biochemistry and Biophysics, Vol. 211, No. 1, 01.10.1981, p. 119-124.

Research output: Contribution to journalArticle

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