Quality Control of Albumin Solutions by Size-Exclusion High-Performance Liquid Chromatography, Isoelectric Focusing, and Two-Dimensional Immunoelectrophoresis

Liedekerke, B.M. Van; Nelis, Hans; Kint, J.; Vanneste, Franck W.; Leenheer, A.P. De

doi:10.1002/jps.2600800104

Cited by 20 publications

(5 citation statements)

References 15 publications

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“…Up to 10% of albumin solutions may be constituted by high-molecular-weight substances. This means that 1g polymers/aggregates can be infused in a patient receiving 50ml of 20% albumin [30,31]. …”

Section: Problems Associated With Albumin Administrationmentioning

confidence: 99%

Untitled

Pulimood

Park

2000

Crit Care

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The benefit of albumin administration in the critically ill patient is unproven. Epidemiological evidence suggests that there is an increase in death among patients with burns, hypoalbuminaemia, and hypotension treated with human albumin solution (HAS). In critical illness, hypoalbuminaemia is a result of transcapillary leak, decreased synthesis, large volume body fluid losses and dilution caused by fluid resuscitation. When treating patients with hypoalbuminaemia, efforts must be centred around correction of the underlying disorder rather than reversal of hypoalbuminaemia. Problems with using albumin arise because it is an expensive blood product, and can result in systemic changes that include cardiovascular, haematological, renal, pulmonary, and immunological effects. The electronic version of the accompanying article can be found online at

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Section: Problems Associated With Albumin Administrationmentioning

confidence: 99%

Untitled

Pulimood

Park

2000

Crit Care

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“…Moreover, current HSA affinity purification, e.g., those relying on Cibacron Blue Sepharose beads (4-7) and/or conventional chromatography (ion exchange, hydrophobic interaction), do not yield highly pure and correctly folded HSA, making more effective purification schemes desirable (1,2).…”

Section: Introductionmentioning

confidence: 99%

“…Because patients often receive large quantities of HSA in a single treatment, commercial HSA preparations require a higher degree of purity than other protein therapeutics. Even under these restrictions, commercial albumin preparations (colloid solutions) contain many impurities (1,2) that may cause adverse side effects in patients (3).…”

Section: Introductionmentioning

confidence: 99%

Development of Mammalian Serum Albumin Affinity Purification Media by Peptide Phage Display

Sato¹,

Sexton²,

Morganelli³

et al. 2002

Biotechnology Progress

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Several phage isolates that bind specifically to human serum albumin (HSA) were isolated from disulfide-constrained cyclic peptide phage-display libraries. The majority of corresponding synthetic peptides bind with micromolar affinity to HSA in low salt at pH 6.2, as determined by fluorescence anisotropy. One of the highest affinity peptides, DX-236, also bound well to several mammalian serum albumins (SA). Immobilized DX-236 quantitatively captures HSA from human serum; mild conditions (100 mM Tris, pH 9.1) allow release of HSA. The DX-236 affinity column bound HSA from human serum with a greater specificity than does Cibacron Blue agarose beads. In addition to its likely utility in HSA and other mammalian SA purifications, this peptide media may be useful in the proteomics and medical research markets for selective removal of mammalian albumin from serum prior to mass spectrometric and other analyses.

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“…16 Several HPLC methods for the determination of HSA have been described, mostly based on size exclusion, ion exchange, and reverse phase (RP) separation. [17][18][19][20][21] This paper describes the development and validation of an RP-HPLC method, which allows quick (10 min) and reliable determination of HSA content in medical devices. The obtained data are used in-house for quality control (QC) purposes, including product release and stability studies.…”

Section: Introductionmentioning

confidence: 99%