Abstract
The action of lecithin cholesterol acyltransferase (LCAT) was studied on an abnormal lipoprotein (LP-X) rich in phosphatidylcholine and cholesterol from the plasma of patients with obstructive liver disease. 60 mg LP-X isolated free of other lipoproteins and subsequently labelled with 3H-cholesterol were incubated with 1 mg highly purified enzyme in the presence of albumin. After 45 h at 37° C, the incubation mixture was subjected to zonal ultracentrifugation. 3H-cholesterol and 3H-cholesteryl esters were quantified in each fraction of the zonal gradient. More than 95% of the lipoproteins in this mixture banded in the density range of LP-X with no change in size distribution, but did contain 593 nmoles of newly formed cholesteryl esters. Agarose electrophoresis revealed an α-migrating band in addition to the original β-band. Also, on agar, the typically cathode migrating LP-X was changed to anode moving material. These studies indicate that LP-X can serve as a substrate for LCAT.
Original language | English (US) |
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Pages (from-to) | 213-217 |
Number of pages | 5 |
Journal | European Journal of Clinical Investigation |
Volume | 7 |
Issue number | 3 |
DOIs | |
State | Published - Jun 1977 |
ASJC Scopus subject areas
- Biochemistry
- Clinical Biochemistry