Frohlich_1982_Clin.Biochem_15_269

Reference

Title : Lecithin: cholesterol acyl transferase (LCAT) - Frohlich_1982_Clin.Biochem_15_269
Author(s) : Frohlich J , McLeod R , Hon K
Ref : Clinical Biochemistry , 15 :269 , 1982
Abstract :

Esterification of cholesterol in plasma is mediated by LCAT. The mechanism of the three reactions catalysed by the enzyme is beginning to be understood. LCAT has been purified from human plasma and partially characterized. The enzyme is closely associated with HDL and exists most likely as a complex with its activator apo A-I and apo D. Antibodies were raised against LCAT and the enzyme concentration in plasma has been estimated to range between 4.5 and 8.0 mg/L. In patients with familial LCAT deficiency only trace amounts or no LCAT protein is found. Heterozygotes for this disorder have approximately half the normal amount of the enzyme. LCAT reactivity is essential for normal lipoprotein metabolism and for a proper equilibrium between tissue and plasma cholesterol.

PubMedSearch : Frohlich_1982_Clin.Biochem_15_269
PubMedID: 6762928
Gene_locus related to this paper: human-LCAT

Related information

Gene_locus human-LCAT

Citations formats

Frohlich J, McLeod R, Hon K (1982)
Lecithin: cholesterol acyl transferase (LCAT)
Clinical Biochemistry 15 :269

Frohlich J, McLeod R, Hon K (1982)
Clinical Biochemistry 15 :269