Effective removal of albumin from serum

Colantonio, David; Dunkinson, C.E.; Bovenkamp, Diane E.; Eyk, Jennifer E. Van

doi:10.1002/pmic.200401235

Cited by 97 publications

(84 citation statements)

References 11 publications

(5 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…There are two primary methods available for isolating albumin from serum: affinity-based (e.g., antibody, cibacron blue) and chemical-based methods (e.g., NaCl/EtOH [9,10] TCA/ acetone [11]). Many of the affinity-based methods have been compared and shown to effectively remove albumin [7,12,13].…”

Section: Introductionmentioning

confidence: 99%

“…Many of the affinity-based methods have been compared and shown to effectively remove albumin [7,12,13]. However, these methods are vulnerable to non-specific binding of proteins/peptides to the ligand and column materials and carryover between experiments in the case of LC columns [7,10,[12][13][14][15]. Alternatively, albumin has been purified using NaCl/EtOH since the 1940s [16] and this method is routinely used for isolating pharmaceutical grade albumin.…”

Section: Introductionmentioning

confidence: 99%

“…Unfortunately, dyebased methods are not sufficiently specific for albumin as it also binds NAD, FAD, and ATPbinding sites on proteins [18,19] and therefore, cannot be used for definitively examining albumin-bound proteins [9,10,14,20,21]. Furthermore, the shortcomings of focusing only on low MW species for biomarker discovery have recently been presented, namely, that the majority of the peptides in this MW range are from highly abundant species [22], not low abundance biomarkers.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Investigation of an albumin‐enriched fraction of human serum and its albuminome

Gundry

Jelinek

et al. 2007

Proteomics Clinical Apps

Self Cite

176

128

View full text Add to dashboard Cite

The removal of albumin and other high abundance proteins is a routine first step in the analysis of serum and plasma proteomes. However, as albumin can bind proteins and peptides, there is a universal concern as to how the serum proteome is changed by the removal of albumin. To address this concern, the current study was designed to identify proteins and peptides removed from the serum during albumin depletion; to determine which of these are bound to albumin (rather than copurified) and whether the bound proteins are intact proteins or peptide fragments. Sequential, independent analyses including both anti-albumin antibody (anti-HSA) affinity chromatography and SEC were used to isolate albumin-bound proteins. RP-HPLC and 1-D SDS-PAGE were then used to further separate the proteins prior to identification by MS/MS. Finally, whole protein molecular weight (MW) MS measurements coupled with protein coverage obtained by MS were combined to assess whether the bound proteins were intact or peptide fragments. Combining the results from multiple approaches, 35 proteins, of which 24 are intact, were found to be associated with albumin, and they include both known high and low abundance proteins.

show abstract

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Investigation of an albumin‐enriched fraction of human serum and its albuminome

Gundry

Jelinek

et al. 2007

Proteomics Clinical Apps

Self Cite

176

128

View full text Add to dashboard Cite

show abstract

“…We have not removed plasma proteins from the samples. Many studies have used methods for precipitation, centrifugation, and affinity chromatography to remove albumin and immunoglobulin (Chen et al, 2005;Colantonio et al, 2005;Zolotarjova et al, 2005). However, these immunodepletion methods have a limited capacity to bind these profuse proteins; thus, depletion is not complete.…”

Section: -Dementioning

confidence: 99%

Comparative proteomic analysis of ductal and lobular invasive breast carcinoma

Oliveira¹,

Gomig²,

Milioli³

et al. 2016

Genet. Mol. Res.

View full text Add to dashboard Cite

ABSTRACT. Breast cancer is the second most common cancer worldwide and the first among women. Invasive ductal carcinoma (IDC) and invasive lobular carcinoma (ILC) are the two major histological subtypes, and the clinical and molecular differences between them justify the search for new markers to distinguish them. As proteomic analysis allows for a powerful and analytical approach to identify potential biomarkers, we performed a comparative analysis of IDC and ILC samples by using two-dimensional electrophoresis and mass spectrometry. Twenty-three spots were identified corresponding to 10 proteins differentially expressed between the two subtypes. ACTB, ACTG, TPM3, TBA1A, TBA1B, VIME, TPIS, PDIA3, PDIA6, and VTDB were upregulated in ductal carcinoma compared to in lobular carcinoma samples. Overall, these 10 proteins have a key role in oncogenesis. Their specific functions and relevance in cancer initiation and progression are further discussed in this study. The identified peptides represent promising biomarkers for the differentiation of ductal and lobular breast cancer subtypes, and for future interventions based on tailored therapy.

show abstract

“…Only four proteins (albumin, transferrin, haptoglobulin and immunoglobulins) make up more than 90% of the protein mass in the blood (7). Although techniques exist for depleting these proteins from the serum (18,19), challenges remain to assure their efficiency and specificity.…”

Section: Proteomics: General Considerationsmentioning

confidence: 99%