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Monitoring the oxidative modification of lipoprotein(a) by capillary zone electrophoresis
Author(s) -
Zinellu Angelo,
Sotgia Salvatore,
Usai Maria Franca,
Deiana Luca,
Carru Ciriaco
Publication year - 2006
Publication title -
european journal of lipid science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.614
H-Index - 94
eISSN - 1438-9312
pISSN - 1438-7697
DOI - 10.1002/ejlt.200500333
Subject(s) - capillary electrophoresis , oxidative phosphorylation , chemistry , lipoprotein , electrophoresis , apolipoprotein b , chromatography , lipoprotein(a) , gel electrophoresis , low density lipoprotein , disulfide bond , biochemistry , cholesterol
Abstract Lipoprotein(a) [Lp(a)] is a recognized risk factor for atherosclerotic cardiovascular disease. It is made of a lipoprotein particle containing apoB100 linked by a single disulfide bridge to apolipoprotein(a), a glycosylated protein with a variable mass. Some authors suggest that oxidative modification could explain the contribution of Lp(a) in the development of atheromatous lesions in a comparable way to low‐density lipoproteins (LDL). Recently, the use of capillary electrophoresis to measure the variations in the relative electrophoretic mobility (REM) of LDL subjected to copper oxidation has been proposed. The aim of this work is to employ this method also to monitor the copper‐induced oxidative modification of Lp(a). Migration of Lp(a) was monitored by absorption at 200 nm in a 50 mmol/L tricine, 100 mmol/L methylglucamine, pH 9.7 run buffer. Contrary to the conventional slab gel methods, our procedure provides a rapid and reproducible means to measure the electrophoretic mobility of Lp(a) (migration time <10 min with a CV% <0.5).