A study of the interaction of lecithin: Cholesterol acyltransferase with subfractions of high density lipoproteins

M. Jahani, A. G. Lacko

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

High density lipoproteins (HDL) were isolated by a chromatographic procedure and subsequently fractionated on a DEAE cellulose (DE-52) column. Four fractions were separated and analyzed for lipid and protein composition and molecular weight. During ion exchange chromatography, one of the four fractions consistently coincided with lecithin:cholesterol acyltransferase (LCAT) activity. When the HDL fractions were incubated with highly purified LCAT preparations, the LCAT activity showed a dependence on unesterified cholesterol concentrations. The HDL subfraction eluting at the highest ionic strength was found to be the best substrate for LCAT. This subfraction exhibited apoprotein and lipid composition similar to HDL3 and contained 31% of the total apoprotein D present in all the subfractions. A positive correlation was found between LCAT activity and the cholesteryl ester/unesterified cholesterol ratio, and a negative correlation was found between LCAT substrate potential and apparent molecular weight of the HDL subfractions when these subfractions were incubated with LCAT. No correlation was apparent between LCAT activity, and the phospholipid/unesterified cholesterol ratio or with the apoA-I/apoA-II ratio.

Original languageEnglish
Pages (from-to)1102-1110
Number of pages9
JournalJournal of Lipid Research
Volume22
Issue number7
StatePublished - 1 Dec 1981

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Phosphatidylcholine-Sterol O-Acyltransferase
HDL Lipoproteins
Apoproteins
Cholesterol
Molecular Weight
Molecular weight
Apolipoprotein A-II
Lipids
DEAE-Cellulose
Cholesterol Esters
Apolipoprotein A-I
Ion Exchange Chromatography
Substrates
Chromatography
Ionic strength
Chemical analysis
Osmolar Concentration
Phospholipids
Ion exchange

Cite this

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abstract = "High density lipoproteins (HDL) were isolated by a chromatographic procedure and subsequently fractionated on a DEAE cellulose (DE-52) column. Four fractions were separated and analyzed for lipid and protein composition and molecular weight. During ion exchange chromatography, one of the four fractions consistently coincided with lecithin:cholesterol acyltransferase (LCAT) activity. When the HDL fractions were incubated with highly purified LCAT preparations, the LCAT activity showed a dependence on unesterified cholesterol concentrations. The HDL subfraction eluting at the highest ionic strength was found to be the best substrate for LCAT. This subfraction exhibited apoprotein and lipid composition similar to HDL3 and contained 31{\%} of the total apoprotein D present in all the subfractions. A positive correlation was found between LCAT activity and the cholesteryl ester/unesterified cholesterol ratio, and a negative correlation was found between LCAT substrate potential and apparent molecular weight of the HDL subfractions when these subfractions were incubated with LCAT. No correlation was apparent between LCAT activity, and the phospholipid/unesterified cholesterol ratio or with the apoA-I/apoA-II ratio.",
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A study of the interaction of lecithin : Cholesterol acyltransferase with subfractions of high density lipoproteins. / Jahani, M.; Lacko, A. G.

In: Journal of Lipid Research, Vol. 22, No. 7, 01.12.1981, p. 1102-1110.

Research output: Contribution to journalArticle

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T2 - Cholesterol acyltransferase with subfractions of high density lipoproteins

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AB - High density lipoproteins (HDL) were isolated by a chromatographic procedure and subsequently fractionated on a DEAE cellulose (DE-52) column. Four fractions were separated and analyzed for lipid and protein composition and molecular weight. During ion exchange chromatography, one of the four fractions consistently coincided with lecithin:cholesterol acyltransferase (LCAT) activity. When the HDL fractions were incubated with highly purified LCAT preparations, the LCAT activity showed a dependence on unesterified cholesterol concentrations. The HDL subfraction eluting at the highest ionic strength was found to be the best substrate for LCAT. This subfraction exhibited apoprotein and lipid composition similar to HDL3 and contained 31% of the total apoprotein D present in all the subfractions. A positive correlation was found between LCAT activity and the cholesteryl ester/unesterified cholesterol ratio, and a negative correlation was found between LCAT substrate potential and apparent molecular weight of the HDL subfractions when these subfractions were incubated with LCAT. No correlation was apparent between LCAT activity, and the phospholipid/unesterified cholesterol ratio or with the apoA-I/apoA-II ratio.

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