2010
DOI: 10.1016/j.jchromb.2010.03.006
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Depletion of highly abundant proteins in blood plasma by hydrophobic interaction chromatography for proteomic analysis

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Cited by 26 publications
(18 citation statements)
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References 31 publications
(40 reference statements)
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“…They found that the combination of the two methods had the potential to remove the highly abundant proteins from plasma, in particular albumin, immunoglobulins, alpha-1-antitrypsin, haptoglobin, and fibrinogen. Because of the simplicity and cost-effectiveness of this process, it could be a good alternative to antibody based methods [72,73]. Brgles et al utilized the principles of displacement chromatography for plasma fractionation and the isolation of low abundance proteins.…”
Section: Non-affinity-based Depletion Methodsmentioning
confidence: 99%
“…They found that the combination of the two methods had the potential to remove the highly abundant proteins from plasma, in particular albumin, immunoglobulins, alpha-1-antitrypsin, haptoglobin, and fibrinogen. Because of the simplicity and cost-effectiveness of this process, it could be a good alternative to antibody based methods [72,73]. Brgles et al utilized the principles of displacement chromatography for plasma fractionation and the isolation of low abundance proteins.…”
Section: Non-affinity-based Depletion Methodsmentioning
confidence: 99%
“…In order to overcome the disadvantages of affinity chromatography for its use in blood plasma proteomics, several complementary strategies have been examined, such as sequential anion and cation exchange chromatography followed by 2DGE; and strong cation exchange chromatography followed by liquid-phase isoelectric focusing (Ottens et al, 2005;Barnea et al, 2005). Since these approaches considerably improve the capacity to detect low abundance proteins, it was suggested that the optimization of combinatorial processes by coupling immuno-affinity depletion with other conventional separation methods such as hydrophobic interaction chromatography will probably lead to significant advances in proteomics (Mahn et al, 2010). Despite the research conducted in this area, there is still a lack of optimized processes that ensure detection of the complete proteome of a tissue or cell.…”
Section: Proteomicsmentioning
confidence: 99%
“…On the other hand, a HIC matrix consisting of highly acetylated agarose has been used for the isolation of immunoglobulin from porcine serum, with a relative success (Ramos-Clamont et al, 2006). Recently, Mahn et al (2010) investigated if the performance of 2DGE could be improved by fractionating blood plasma through a HIC step, thus reducing the relative concentration of some highly abundant proteins in plasma. First, the hydrophobicity of the main 56 proteins present in blood plasma was determined.…”
Section: Plasma Fractionation By Hicmentioning
confidence: 99%
“…There are a number of labs that have reported on the use of technologies, the most common of which are for albumin [7][8][9] and immunoglobulins (IgA/G) [5,10]. This depletion format is very efficient at removing the targeted protein, or protein class; however, they are limiting when a more encompassing depletion strategy is required.…”
Section: Introductionmentioning
confidence: 99%