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Abstracts of Oak Ridge Posters |
(1 Department of Chemistry "G. Ciamician", Bologna, Italy; 2 Wyatt Technology Europe GmbH, Dernbach, Germany;
aaddress correspondence to this author at: Department of Chemistry "G. Ciamician", Via Selmi 2, 40126 Bologna, Italy; fax 39-0-51-2099452, e-mail pierluig.reschiglian@unibo.it)
| The first 300 words of the full text of this article appear below. |
Determination of total cholesterol (TC), HDL and LDL cholesterol, and triglycerides (TG) is used to assess lipoprotein abnormalities and coronary artery disease (CAD) risk. Furthermore, studies have demonstrated that small, dense LDL particles penetrate more easily into the arterial intima (1), exhibit increasing binding to arterial wall proteoglycans(2), and are more prone to oxidative stress(3). Small, dense LDL particles also have a prolonged plasma half-life because of their lower binding affinity for the LDL receptor(4). The presence of small, dense LDL particles in plasma is, therefore, considered to be proatherogenic.
Analytical methods for LDL size characterization are therefore expected to improve classification, diagnosis, and therapy of dyslipidemic patients. However, simple methods for routine LDL size measurement are not yet available. LDL size is mainly measured by nondenaturing PAGE (5), which is time-consuming and may be unsuitable for large numbers of samples. Easier methods for measuring LDL size have been proposed, including high-performance gel-filtration chromatography (HPGC)(6). Both PAGE and HPGC can give accurate size estimations only if appropriate standards are available. Moreover, recent studies have shown that LDL particles may be discoidal, with diameter and height that are not significantly correlated(7). PAGE and HPGC cannot give information on particle conformation.
Flow field-flow fractionation (FlFFF) is a separation technique in which macromolecules and particles are separated by the combined actions of an axial flow and a perpendicular cross-flow (8). No stationary phase is present, and the separation mechanism is sufficiently gentle not to alter the native structure of proteins and protein complexes(9). Proteins are fractionated according to their difference in diffusion, with retention time that is inversely proportional to the analyte diffusion coefficient. In principle, with the use of FlFFF it is possible to
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