Separation and selective detection of lipoprotein particles of patients with coronary artery disease by frit-inlet asymmetrical flow field-flow fractionation

Park, Ilyong; Paeng, Ki‐Jung; Yoon, Yeomin; Song, Jung Han; Moon, Myeong Hee

doi:10.1016/s1570-0232(02)00630-x

Cited by 52 publications

(32 citation statements)

References 23 publications

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“…(2), the Stokes' diameter of LDL from the CAD patient sample, determined in correspondence of the retention time of the LDL fractogram maximum, was calculated to be 21.8 nm. This size value is in very good agreement with the size value (21.6 nm) observed in the earlier report on FI AFlFFF of lipoproteins [19]. The Stokes' diameter of LDL determined from the healthy donor person was 23.2 nm.…”

Section: Methodssupporting

confidence: 91%

“…Lipoproteins contained in human blood plasma from healthy donors and from patients with CAD were considered. In an earlier study, FI AFlFFF was applied for identifying the decrease of particle size of low density lipoproteins (LDL) as well as the decrease of amount of high density lipoproteins (HDL) in blood plasma from patients with CAD [19]. It therein highlighted the potential application of FlFFF for clinical diagnosis by calculating LDL sizes from the FlFFF elution peak through a direct injection of plasma.…”

Section: Methodsmentioning

confidence: 99%

“…Plasma samples were stained prior to injection with Sudan Black B, which is a specific dye for lipid components in lipoproteins, and detection was made at 595 nm. In the earlier work [19], direct monitoring of the lipoproteins at 280 nm without staining was proven to be nonselective because of the interference of high-abundance serum proteins. In the upper fractograms of Fig.…”

Section: Methodsmentioning

confidence: 99%

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Performance of hollow‐fiber flow field‐flow fractionation in protein separation

Park

Paeng

Kang

et al. 2005

J of Separation Science

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Since hollow-fiber flow field-flow fractionation (HF FIFFF) utilizes a cylindrical channel made of a hollow-fiber membrane, which is inexpensive and simple in channel assembly and thus disposable, interests are increasing as a potential separation device in cells, proteins, and macromolecules. In this study, performance of HF FIFFF of proteins is described by examining the influence of flow rate conditions and length of fiber (polyacrylonitrile or PAN in this work) on sample recovery as well as experimental plate heights. The interfiber reproducibility in terms of separation time and recovery was also studied. Experiments showed that sample recovery was consistent regardless of the length of fiber when the effective field strength (equivalent to the mean flow velocity at the fiber wall) and the channel void time were adjusted to be equivalent for channels of various fiber lengths. This supported that the majority of sample loss in HF FIFFF separation of apoferritin and their aggregates may occur before the migration process. It is finally demonstrated that HF FIFFF can be applied for characterizing the reduction in Stokes' size of low density lipoproteins from blood plasma samples obtained from patients having coronary artery disease and from healthy donors.

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Section: Methodssupporting

confidence: 91%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Performance of hollow‐fiber flow field‐flow fractionation in protein separation

Park

Paeng

Kang

et al. 2005

J of Separation Science

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“…Low levels of HDL and high levels of LDL are purported to increase the risk of CAD, and FlFFF-based studies of lipoproteins have shown that, compared to control sets of healthy individuals, the size of LDLs decreases among patients with CAD; concurrently, there is an increase in LDL concentration [25]. Using MxHF5, the separated lipoproteins from healthy controls and patients with CAD were collected, after which the lipids within them were extracted and characterized using nLC-ESI-MS/MS [26].…”

Section: Investigation Of Phospholipids From Lipoproteins Of Patientsmentioning

confidence: 99%

Flow Field-Flow Fractionation with Mass Spectrometry for Top-Down and Bottom-Up Lipidomics

Byeon

Moon

2017

J. Anal. Test.

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As lipidomics has attracted increased attention in life science, advanced mass spectrometry (MS) technologies have been combined with other separation techniques to improve and expand the branch of study. This review intends to provide general knowledge of offline and online coupling of flow field-flow fractionation (FlFFF)-a technique that encompasses the separation of nano-to micro-scale biomolecules-with MS for analysis of blood plasma lipoproteins, processes that are considered bottomup and top-down approaches, respectively. The first part of this review focuses on the bottom-up method using multiplexed hollow fiber FlFFF (MxHF5) and nanoflow liquid chromatography electrospray-ionization tandem mass spectrometry (nLC-ESI-MS/MS) for non-targeted identification of lipids. In this protocol, plasma lipoproteins of different types are collected using MxHF5, and the lipids within the lipoproteins are then extracted and analyzed via nLC-ESI-MS/MS. The second part of the review describes the top-down approach, which uses online coupling of miniaturized FlFFF to ESI-MS for a fast screening of targeted lipids. Here, the separation of lipoproteins and detection of their component lipids are achieved simultaneously. While both methods aim to quantify the lipids within lipoproteins, the bottom-up approach provides an extensive lipidome, whereas the top-down method is suitable for high-speed targeted lipidomic analysis. This review discusses variants of FlFFF-ESI-MS/MS that offer effective analytical technologies for lipidomics.

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“…FlFFF was subsequently used to separate additional proteins [2], wheat proteins, monitor lipoprotein particle size distributions for potential use as a biomarker for the coronary artery disease [69], and investigate protein and DNA (linear and circular) conformation [70,71]. These earlier studies were conducted with on-line UV detectors and relied upon developed FFF theory or calibration curves for transformation of the time-based fractograms into size or MW distributions.…”

Section: Proteins Protein Aggregates and Dnamentioning

confidence: 99%

Field‐flow fractionation of proteins, polysaccharides, synthetic polymers, and supramolecular assemblies

Williams¹,

Lee

2006

J of Separation Science

125

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This review summarizes developments and applications of flow and thermal field-flow fractionation (FFF) in the areas of macromolecules and supramolecular assemblies. In the past 10 years, the use of these FFF techniques has extended beyond determining diffusion coefficients, hydrodynamic diameters, and molecular weights of standards. Complex samples as diverse as polysaccharides, prion particles, and block copolymers have been characterized and processes such as aggregation, stability, and infectivity have been monitored. The open channel design used in FFF makes it a gentle separation technique for high- and ultrahigh-molecular weight macromolecules, aggregates, and self-assembled complexes. Coupling FFF with other techniques such as multiangle light scattering and MS provides additional invaluable information about conformation, branching, and identity.

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Separation and selective detection of lipoprotein particles of patients with coronary artery disease by frit-inlet asymmetrical flow field-flow fractionation

Cited by 52 publications

References 23 publications

Performance of hollow‐fiber flow field‐flow fractionation in protein separation

Performance of hollow‐fiber flow field‐flow fractionation in protein separation

Flow Field-Flow Fractionation with Mass Spectrometry for Top-Down and Bottom-Up Lipidomics

Field‐flow fractionation of proteins, polysaccharides, synthetic polymers, and supramolecular assemblies

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