Biochemical and compositional analyses of recombinant lecithin:cholesterol acyltransferase (LCAT) obtained from a hepatic source
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology
Reference24 articles.
1. Isolation, properties, and mechanism of in vitro action of lecithin: cholesterol acyltransferase from human plasma.
2. Characterization of lecithin–cholesterol acyltransferase from human plasma. 3. Chemical properties of the enzyme
3. Lecithin:cholesterol acyltransferase. Functional regions and a structural model of the enzyme.
4. Lecithin:cholesterol acyltransferase: role of N-linked glycosylation in enzyme function
5. Expression and characterization of recombinant human lecithin:cholesterol acyltransferase
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1. Cholesterol efflux capacity, macrophage reverse cholesterol transport and cardioprotective HDL;Current Opinion in Lipidology;2015-10
2. Recombinant human lecithin-cholesterol acyltransferase Fc fusion: Analysis of N- and O-linked glycans and identification and elimination of a xylose-based O-linked tetrasaccharide core in the linker region;Protein Science;2013-11-12
3. Lecithin: cholesterol acyltransferase – from biochemistry to role in cardiovascular disease;Current Opinion in Endocrinology, Diabetes & Obesity;2009-04
4. A dual role for lecithin:cholesterol acyltransferase (EC 2.3.1.43) in lipoprotein oxidation;Free Radical Biology and Medicine;2007-12
5. Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: An update covering the period 1999–2000;Mass Spectrometry Reviews;2006
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