Thiophilic adsorption revisited☆

Hardouin, Julie; Duchateau, Magalie; Canelle, Ludovic; Vlieghe, Céline; Joubert‐Caron, Raymonde; Caron, Michel

doi:10.1016/j.jchromb.2006.08.017

Cited by 21 publications

(16 citation statements)

References 21 publications

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“…The endcapping of the epoxide group with 2-mercaptoethanol and 2-ethanolamine is visualized in Fig. 2b and c. Both concepts, the coupling of thiophilic ligands as well as amino-functional ligands onto solid supports are state of the art and therefore well discussed in literature [42][43][44]. A comprehensive study dealing with the influence of spacer-chain chemistry and support chemistry on the IgG capture performance of the bio-mimetic ligand A2P from a chromatographic as well as a theoretical thermodynamic viewpoint was recently published [27].…”

Section: Epoxide-activated Support Materialsmentioning

confidence: 96%

Optimization of a ligand immobilization and azide group endcapping concept via “Click-Chemistry” for the preparation of adsorbents for antibody purification

Horak

Hofer

Lindner

2010

Journal of Chromatography B

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Section: Epoxide-activated Support Materialsmentioning

confidence: 96%

Optimization of a ligand immobilization and azide group endcapping concept via “Click-Chemistry” for the preparation of adsorbents for antibody purification

Horak

Hofer

Lindner

2010

Journal of Chromatography B

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“…The proteins from lysed cells are subjected to 2-D immunoaffinity separation according to their affinity for immunoglobulins from healthy controls in the first dimension and immunoglobulins from patients in the second dimension. The affinity supports used during these separations are prepared by coupling an IgG fraction isolated from the sera of healthy volunteers (first dimension) or patients (second dimension) (41). The first immunoaffinity chromatography is crucial as it is used for selectively removing proteins (autoantigens) recognized by healthy volunteers' antibodies.…”

Section: Multiple Affinity Protein Profilingmentioning

confidence: 99%

Cancer Immunomics Using Autoantibody Signatures for Biomarker Discovery

Caron

Choquet-Kastylevsky

Joubert‐Caron

2007

Molecular & Cellular Proteomics

140

127

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The increased incidence of autoantibodies in malignancies has been described since the 1970s. Thus the ability to determine molecular fingerprinting of autoantibodies (antibody signatures) may provide useful clinical diagnostic and prognostic information. This review describes the use of several proteomics approaches for the identification of antigens recognized by these autoantibodies. Serological proteome analysis combines separation of tumor cell proteins on two-dimensional gel electrophoresis gels, Western blotting with sera of patients and healthy subjects, and identification of the detected antigens by MS. Alternatively multiple affinity protein profiling combines isolation of the antigens recognized by patient antibodies by two-dimensional immunoaffinity chromatography and identification by MS/MS. The use and limitations of reverse phase protein microarrays for testing patient serum containing autoantibodies are also considered. Lastly

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“…Immunoglobulin G (IgG) fractions were isolated from sera obtained from eight healthy volunteers as previously described [16]. Before using a column, washing was carried out with 1 CV of elution buffer at 0.8 mL/min and the column was then equilibrated by the washing buffer for an additional 2 CV.…”

Section: Preparation Of Immunoaffinity Supports and Purification Of Amentioning

confidence: 99%

HPLC‐chip‐mass spectrometry for protein signature identifications

Hardouin¹,

Joubert‐Caron

Caron

2007

J of Separation Science

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This work investigates the use of an HPLC-chip microfluidic device interfaced to an IT mass spectrometer to search for biomarker signatures. To that end, the identification of autoantigens is chosen as a model. It not only constitutes a proof of concept model but also the growing interest in autoantibodies and autoantigens as new markers of diseases provides a practical application at the same time. The peptides are separated by the HPLC-chip system allowing suitable resolution and reproducibility. The determination of two parameters that characterize a peptide sequence during LC-MS/MS analyses, retention time (RT) and m/z ratio, improves the identification of a number of peptides derived from protein digests. These findings illustrate that accurate RT measurement obtained in a microfluidic device is useful to obtain mass/retention time (MRT) pairs for a given peptide, which can contribute to the definition of biomarker signatures.

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Thiophilic adsorption revisited☆

Cited by 21 publications

References 21 publications

Optimization of a ligand immobilization and azide group endcapping concept via “Click-Chemistry” for the preparation of adsorbents for antibody purification

Optimization of a ligand immobilization and azide group endcapping concept via “Click-Chemistry” for the preparation of adsorbents for antibody purification

Cancer Immunomics Using Autoantibody Signatures for Biomarker Discovery

HPLC‐chip‐mass spectrometry for protein signature identifications

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