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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...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Molecular Diversity Preservation International (MDPI)
2012
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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. |
format | Online Article Text |
id | pubmed-3546697 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Molecular Diversity Preservation International (MDPI) |
record_format | MEDLINE/PubMed |
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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