Lipoprotein‐X: a substrate for lecithin: cholesterol acyltransferase

JOSEF R. PATSCH, ANNE K. SOUTAR, JOEL D. MORRISETT, ANTONIO M. GOTTO, LOUIS C. SMITH

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

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 languageEnglish (US)
Pages (from-to)213-217
Number of pages5
JournalEuropean Journal of Clinical Investigation
Volume7
Issue number3
DOIs
StatePublished - Jun 1977

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry

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