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Lipoprotein‐X: a substrate for lecithin: cholesterol acyltransferase
Author(s) -
PATSCH JOSEF R.,
SOUTAR ANNE K.,
MORRISETT JOEL D.,
GOTTO ANTONIO M.,
SMITH LOUIS C.
Publication year - 1977
Publication title -
european journal of clinical investigation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.164
H-Index - 107
eISSN - 1365-2362
pISSN - 0014-2972
DOI - 10.1111/j.1365-2362.1977.tb01600.x
Subject(s) - lecithin , chemistry , cholesterol , chromatography , lipoprotein , sterol o acyltransferase , phosphatidylcholine , albumin , cholesteryl ester , substrate (aquarium) , biochemistry , acyltransferase , agarose , enzyme , phospholipid , biology , ecology , membrane
. 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 3 H‐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. 3 H‐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.