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  Nitration of the Birch Pollen Allergen Bet v 1.0101: Efficiency and Site-Selectivity of Liquid and Gaseous Nitrating Agents

Reinmuth-Selzle, K., Ackaert, C., Kampf, C. J., Samonig, M., Shiraiwa, M., Kofler, S., et al. (2014). Nitration of the Birch Pollen Allergen Bet v 1.0101: Efficiency and Site-Selectivity of Liquid and Gaseous Nitrating Agents. Journal of Proteome Research, 13(3), 1570-1577. doi:10.1021/pr401078h.

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Reinmuth-Selzle, Kathrin1, Autor           
Ackaert, Chloe2, Autor
Kampf, Christopher J.1, Autor           
Samonig, Martin2, Autor
Shiraiwa, Manabu1, Autor           
Kofler, Stefan2, Autor
Yang, Hong1, Autor           
Gadermaier, Gabriele2, Autor
Brandstetter, Hans2, Autor
Huber, Christian G.2, Autor
Duschl, Albert2, Autor
Oostingh, Gertie J.2, Autor
Pöschl, Ulrich1, Autor           
Affiliations:
1Multiphase Chemistry, Max Planck Institute for Chemistry, Max Planck Society, ou_1826290              
2external, ou_persistent22              

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 Zusammenfassung: Nitration of the major birch pollen allergen Bet v 1 alters the immune responses toward this protein, but the underlying chemical mechanisms are not yet understood. Here we address the efficiency and site-selectivity of the nitration reaction of recombinant protein samples of Bet v 1.0101 with different nitrating agents relevant for laboratory investigations (tetranitromethane, TNM), for physiological processes (peroxynitrite, ONOO-), and for the health effects of environmental pollutants (nitrogen dioxide and ozone, O-3/NO2). We determined the total tyrosine nitration degrees (ND) and the NDs of individual tyrosine residues (ND). High-performance liquid chromatography coupled to diode array detection and HPLC coupled to high-resolution mass spectrometry analysis of intact proteins, HPLC coupled to tandem mass spectrometry analysis of tryptic peptides, and amino acid analysis of hydrolyzed samples were performed. The preferred reaction sites were tyrosine residues at the following positions in the polypeptide chain: Y83 and Y81 for ONOO-, and Y83 and Y158 for O-3/NO2. The tyrosine residues Y83 and Y81 are located in a hydrophobic cavity, while Y150 and Y158 are located in solvent-accessible and flexible structures of the C-terminal region. The heterogeneous reaction with O-3/ NO2 was found to be strongly dependent on the phase state of the protein. Nitration rates were about one order of magnitude higher for aqueous protein solutions (similar to 20% per day) than for protein filter samples (similar to 2% per day). Overall, our findings show that the kinetics and site-selectivity of nitration strongly depend on the nitrating agent and reaction conditions, which may also affect the biological function and adverse health effects of the nitrated protein.

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 Datum: 2014-03
 Publikationsstatus: Erschienen
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 Ort, Verlag, Ausgabe: -
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 Art der Begutachtung: -
 Identifikatoren: ISI: 000332756300036
DOI: 10.1021/pr401078h
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Titel: Journal of Proteome Research
  Andere : J. Proteome Res.
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Washington, D.C. : American Chemical Society
Seiten: - Band / Heft: 13 (3) Artikelnummer: - Start- / Endseite: 1570 - 1577 Identifikator: ISSN: 1535-3893
CoNE: https://pure.mpg.de/cone/journals/resource/111019664290000