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Polystyrene beads as an alternative support material for epitope identification of a prion-antibody interaction using proteolytic excision mass spectrometry

Polystyrene beads as an alternative support material for epitope identification of a prion-antibody interaction using proteolytic excision mass spectrometry

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Prüfsumme: MD5:3e1b60cdbe1362a667806d33e232986b

PIMENOVA, Tatiana, Lukas MEIER, Bernd ROSCHITZKI, Gabriela PARASCHIV, Michael PRZYBYLSKI, Renato ZENOBI, 2009. Polystyrene beads as an alternative support material for epitope identification of a prion-antibody interaction using proteolytic excision mass spectrometry. In: Analytical and Bioanalytical Chemistry. 395(5), pp. 1395-1401. ISSN 1618-2642. eISSN 1618-2650. Available under: doi: 10.1007/s00216-009-3119-8

@article{Pimenova2009Polys-10002, title={Polystyrene beads as an alternative support material for epitope identification of a prion-antibody interaction using proteolytic excision mass spectrometry}, year={2009}, doi={10.1007/s00216-009-3119-8}, number={5}, volume={395}, issn={1618-2642}, journal={Analytical and Bioanalytical Chemistry}, pages={1395--1401}, author={Pimenova, Tatiana and Meier, Lukas and Roschitzki, Bernd and Paraschiv, Gabriela and Przybylski, Michael and Zenobi, Renato} }

The binding epitope structure of a protein specifically recognized by an antibody provides key information to prevent and treat diseases with therapeutic antibodies and to develop antibody-based diagnostics. Epitope structures of antigens can be effectively identified by the proteolytic epitope excision mass spectrometry (MS) method, which involves (1) immobilization of monoclonal or polyclonal antibodies, e.g., on N-hydroxysuccinimide-activated sepharose, (2) affinity binding of the antigen followed by limited proteolytic digestion of the<br />immobilized immune complex, and (3) elution and mass spectrometric analysis of the remaining affinity-bound peptide(s). In the epitope analysis of recombinant cellular bovine prion protein (bPrPC) to a monoclonal antibody (mAb3E7), we found that epitope excision experiments resulted in extensive nonspecific binding of bPrP to a standard sepharose matrix employed. Here, we show that the use of amino-modified polystyrene beads with aldehyde functionality is an efficient alternative support for antibody immobilization, suitable for epitope excision MS, with complete suppression of nonspecific bPrP binding. Zenobi, Renato application/pdf 2011-03-24T18:15:54Z Meier, Lukas Roschitzki, Bernd Polystyrene beads as an alternative support material for epitope identification of a prion-antibody interaction using proteolytic excision mass spectrometry Zenobi, Renato Roschitzki, Bernd First publ. in: Analytical and Bioanalytical Chemistry, 395 (2009), 5, pp. 1395 1401 Meier, Lukas Przybylski, Michael 2009 Paraschiv, Gabriela 2011-03-24T18:15:54Z Przybylski, Michael Paraschiv, Gabriela Pimenova, Tatiana deposit-license Pimenova, Tatiana eng

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