cholesterol esterase


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Related to cholesterol esterase: Cholesteryl esterase

cholesterol esterase

/cho·les·ter·ol es·ter·ase/ (kah-les´ter-ol es´ter-ās) acid lipase; an enzyme that catalyzes the hydrolytic cleavage of cholesterol and other sterol esters and triglycerides. Deficiency of the lysosomal enzyme causes the allelic disorders Wolman's disease and cholesteryl ester storage disease.

LIPA

A gene on chromosome 10q23.2 that encodes lipase A, the lysosomal acid lipase (i.e., cholesterol ester hydrolase) that catalyses the hydrolysis of cholesteryl esters and triglycerides in lysosomes.

Molecular pathology
LIPA mutations are linked to CESD and Wolman disease.
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Cholesterol esterase and cholesterol oxidase (5 units/ml of each) were added to this mixture and stirred for two minutes at room temperature (25[degrees]C) to achieve a homogenous distribution of enzymes within the polymer.
Cholesterol esterase activity was measured as described below.
A second reagent is added that contains a detergent that forms stable micelles with HDL and the previously stabilized VLDL and chylomicrons and inhibits their reaction with cholesterol esterase and oxidase.
Recently, an electrophoretic method using cholesterol esterase and cholesterol oxidase with aminoethyl carbazole dye was reported (38).
Reagent 2 contains the enzymes cholesterol oxidase and cholesterol esterase, peroxidase, dye, buffer (pH 6.
2+] were found to selectively block but not precipitate chylomicrons and VLDL, providing selectivity without the need for a clearing reagent; and (b) the specificities of the enzymes cholesterol esterase and cholesterol oxidase toward HDL-C were enhanced by covalently linking polyethylene glycol molecules to the enzymes, excluding cholesterol in the larger LDL particles.
They involved releasing the undesirable lipoprotein components by means of several components included in reagent 1 (selective ionic strength buffers, cholesterol esterase, cholesterol oxidase, and catalase).
Automated agarose gel electrophoresis of lipoproteins in alkaline buffer was adapted to allow the direct quantification of cholesterol in each lipoprotein fraction within the gel, using the cholesterol esterase /cholesterol oxidase reaction (SEBIA).
The reaction principle of Accutrend Triglycerides is lipolysis of triglycerides to give free glycerol and fatty acids by the lipase activity of a cholesterol esterase.
Reagent 2 was reconstituted before use and consisted of a lyophilized enzyme mixture containing PEG-modified cholesterol esterase, PEG-modified cholesterol oxidase, peroxidase, and 4-aminoantipyrine (10).
We determined LDL-C on the Cobas FARA (Roche Diagnostic Systems), using cholesterol reagents: cholesterol esterase and oxidase (Boehringer Mannheim Diagnostics) and an LDL-C kit (Sigma Diagnostics).

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