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 language | English |
|---|---|
| Pages (from-to) | 1102-1110 |
| Number of pages | 9 |
| Journal | Journal of Lipid Research |
| Volume | 22 |
| Issue number | 7 |
| State | Published - 1 Dec 1981 |
Fingerprint
Cite this
}
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 journal › Article
TY - JOUR
T1 - A study of the interaction of lecithin
T2 - Cholesterol acyltransferase with subfractions of high density lipoproteins
AU - Jahani, M.
AU - Lacko, A. G.
PY - 1981/12/1
Y1 - 1981/12/1
N2 - 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.
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.
UR - http://www.scopus.com/inward/record.url?scp=0019783066&partnerID=8YFLogxK
M3 - Article
C2 - 7299290
AN - SCOPUS:0019783066
VL - 22
SP - 1102
EP - 1110
JO - Journal of Lipid Research
JF - Journal of Lipid Research
SN - 0022-2275
IS - 7
ER -