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Characterization of in Vitro Modified Human Very Low-Density Lipoprotein Particles and Phospholipids by Capillary Electrophoresis

A simple capillary zone electrophoresis (CZE) method was used to characterize human very low-density lipoprotein (VLDL) particles for four healthy donors. One major peak was observed for native, in vitro oxidized and glycated VLDL particles. The effective mobilities and peak areas of the capillary e...

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Autores principales: Liu, Yi-Ning, Shu, Ting-Yu, Xie, Huai-Guang, Lai, Wei-Ting, Liao, Yi-Han, Su, Mei-Yu, Lin, You-Sian, Chen, Yen-Yi, Lin, Yi-Jyun, Chong, Chin-Pong, Liu, Mine-Yine
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3546697/
https://www.ncbi.nlm.nih.gov/pubmed/23208377
http://dx.doi.org/10.3390/ijms131216400
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author Liu, Yi-Ning
Shu, Ting-Yu
Xie, Huai-Guang
Lai, Wei-Ting
Liao, Yi-Han
Su, Mei-Yu
Lin, You-Sian
Chen, Yen-Yi
Lin, Yi-Jyun
Chong, Chin-Pong
Liu, Mine-Yine
author_facet Liu, Yi-Ning
Shu, Ting-Yu
Xie, Huai-Guang
Lai, Wei-Ting
Liao, Yi-Han
Su, Mei-Yu
Lin, You-Sian
Chen, Yen-Yi
Lin, Yi-Jyun
Chong, Chin-Pong
Liu, Mine-Yine
author_sort Liu, Yi-Ning
collection PubMed
description A simple capillary zone electrophoresis (CZE) method was used to characterize human very low-density lipoprotein (VLDL) particles for four healthy donors. One major peak was observed for native, in vitro oxidized and glycated VLDL particles. The effective mobilities and peak areas of the capillary electrophoresis (CE) profiles showed good reproducibility and precision. The mobility of the oxidized VLDL peak was higher than that of the native VLDL. The mobility of the glycated VLDL peak was similar to that of the native VLDL. Phospholipids isolated from VLDL particles were analyzed by our recently developed micellar electrokinetic chromatography (MEKC) with a high-salt stacking method. At absorbance 200 nm, the native VLDL phospholipids showed a major peak and a minor peak for each donor. For oxidized VLDL phospholipids, the area of the major peak reduced for three donors, possibly due to phospholipid decomposition. For glycated VLDL phospholipids, the peak mobilities were more positive than native VLDL phospholipids for two donors, possibly due to phospholipid-linked advanced glycation end products (AGEs). Very interestingly, at absorbance 234 nm, the major peak of oxidized VLDL phospholipids was resolved as two peaks for each donor, possibly due to conjugated dienes formed upon oxidation.
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spelling pubmed-35466972013-01-23 Characterization of in Vitro Modified Human Very Low-Density Lipoprotein Particles and Phospholipids by Capillary Electrophoresis Liu, Yi-Ning Shu, Ting-Yu Xie, Huai-Guang Lai, Wei-Ting Liao, Yi-Han Su, Mei-Yu Lin, You-Sian Chen, Yen-Yi Lin, Yi-Jyun Chong, Chin-Pong Liu, Mine-Yine Int J Mol Sci Article A simple capillary zone electrophoresis (CZE) method was used to characterize human very low-density lipoprotein (VLDL) particles for four healthy donors. One major peak was observed for native, in vitro oxidized and glycated VLDL particles. The effective mobilities and peak areas of the capillary electrophoresis (CE) profiles showed good reproducibility and precision. The mobility of the oxidized VLDL peak was higher than that of the native VLDL. The mobility of the glycated VLDL peak was similar to that of the native VLDL. Phospholipids isolated from VLDL particles were analyzed by our recently developed micellar electrokinetic chromatography (MEKC) with a high-salt stacking method. At absorbance 200 nm, the native VLDL phospholipids showed a major peak and a minor peak for each donor. For oxidized VLDL phospholipids, the area of the major peak reduced for three donors, possibly due to phospholipid decomposition. For glycated VLDL phospholipids, the peak mobilities were more positive than native VLDL phospholipids for two donors, possibly due to phospholipid-linked advanced glycation end products (AGEs). Very interestingly, at absorbance 234 nm, the major peak of oxidized VLDL phospholipids was resolved as two peaks for each donor, possibly due to conjugated dienes formed upon oxidation. Molecular Diversity Preservation International (MDPI) 2012-12-03 /pmc/articles/PMC3546697/ /pubmed/23208377 http://dx.doi.org/10.3390/ijms131216400 Text en © 2012 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0 This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Liu, Yi-Ning
Shu, Ting-Yu
Xie, Huai-Guang
Lai, Wei-Ting
Liao, Yi-Han
Su, Mei-Yu
Lin, You-Sian
Chen, Yen-Yi
Lin, Yi-Jyun
Chong, Chin-Pong
Liu, Mine-Yine
Characterization of in Vitro Modified Human Very Low-Density Lipoprotein Particles and Phospholipids by Capillary Electrophoresis
title Characterization of in Vitro Modified Human Very Low-Density Lipoprotein Particles and Phospholipids by Capillary Electrophoresis
title_full Characterization of in Vitro Modified Human Very Low-Density Lipoprotein Particles and Phospholipids by Capillary Electrophoresis
title_fullStr Characterization of in Vitro Modified Human Very Low-Density Lipoprotein Particles and Phospholipids by Capillary Electrophoresis
title_full_unstemmed Characterization of in Vitro Modified Human Very Low-Density Lipoprotein Particles and Phospholipids by Capillary Electrophoresis
title_short Characterization of in Vitro Modified Human Very Low-Density Lipoprotein Particles and Phospholipids by Capillary Electrophoresis
title_sort characterization of in vitro modified human very low-density lipoprotein particles and phospholipids by capillary electrophoresis
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3546697/
https://www.ncbi.nlm.nih.gov/pubmed/23208377
http://dx.doi.org/10.3390/ijms131216400
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