@article{LuetkecosmannWarsinkeTschoepeetal.2017,
  author    = {L{\"u}tkecosmann, Steffi and Warsinke, Axel and Tsch{\"o}pe, Winfried and Eichler, R{\"u}diger and Hanack, Katja},
  title     = {A novel monoclonal antibody suitable for the detection of leukotriene B4},
  series = {Biochemical and biophysical research communications},
  volume    = {482},
  journal   = {Biochemical and biophysical research communications},
  number    = {4},
  publisher = {Elsevier},
  address   = {San Diego},
  issn      = {0006-291X},
  doi       = {10.1016/j.bbrc.2016.11.157},
  pages     = {1054 -- 1059},
  year      = {2017},
  abstract  = {Leukotriene B4 as an inflammatory mediator is an important biomarker for different respiratory diseases like asthma, chronic obstructive pulmonary disease or cystic lung fibrosis. Therefore the detection of LTB4 is helpful in the diagnosis of these pulmonary diseases. However, until now its determination in exhaled breath condensates suffers from problems of accuracy. Reasons for that could be improper sample collection and preparation methods of condensates and the lack of consistently assay specificity and reproducibility of the used immunoassay detection system. In this study we describe the development and the characterization of a specific monoclonal antibody (S27BC6) against LTB4, its use as molecular recognition element for the development of an enzyme-linked immunoassay to detect LTB4 and discuss possible future diagnostic applications.},
  language  = {en}
}
@article{EisoldKupstatKlieretal.2014,
  author    = {Eisold, Ursula and Kupstat, Annette and Klier, Dennis Tobias and Primus, Philipp-A. and Pschenitza, Michael and Niessner, Reinhard and Knopp, Dietmar and Kumke, Michael Uwe},
  title     = {Probing the physicochemical interactions of 3-hydroxy-benzo[a]pyrene with different monoclonal and recombinant antibodies by use of fluorescence line-narrowing spectroscopy},
  series = {Analytical \& bioanalytical chemistry},
  volume    = {406},
  journal   = {Analytical \& bioanalytical chemistry},
  number    = {14},
  publisher = {Springer},
  address   = {Heidelberg},
  issn      = {1618-2642},
  doi       = {10.1007/s00216-013-7584-8},
  pages     = {3387 -- 3394},
  year      = {2014},
  abstract  = {Characterization of interactions between antigens and antibodies is of utmost importance both for fundamental understanding of the binding and for development of advanced clinical diagnostics. Here, fluorescence line-narrowing (FLN) spectroscopy was used to study physicochemical interactions between 3-hydroxybenzo[a]pyrene (3OH-BaP, as antigen) and a variety of solvent matrices (as model systems) or anti-polycyclic aromatic hydrocarbon antibodies (anti-PAH). We focused the studies on the specific physicochemical interactions between 3OH-BaP and different, previously obtained, monoclonal and recombinant anti-PAH antibodies. Control experiments performed with non-binding monoclonal antibodies and bovine serum albumin (BSA) indicated that nonspecific interactions did not affect the FLN spectrum of 3OH-BaP. The spectral positions and relative intensities of the bands in the FLN spectra are highly dependent on the molecular environment of the 3OH-BaP. The FLN bands correlate with different vibrational modes of 3OH-BaP which are affected by interactions with the molecular environment (pi-pi interactions, H-bonding, or van-der-Waals forces). Although the analyte (3OH-BaP) was the same for all the antibodies investigated, different binding interactions could be identified from the FLN spectra on the basis of structural flexibility and conformational multiplicity of the antibodies' paratopes.},
  language  = {en}
}
@article{KuhneDippongFlemigetal.2014,
  author    = {Kuhne, Maren and Dippong, Martin and Flemig, Sabine and Hoffmann, Katrin and Petsch, Kristin and Schenk, J{\"o}rg A. and Kunte, Hans-J{\"o}rg and Schneider, Rudolf J.},
  title     = {Comparative characterization of mAb producing hapten-specific hybridoma cells by flow cytometric analysis and ELISA},
  series = {Journal of immunological methods},
  volume    = {413},
  journal   = {Journal of immunological methods},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0022-1759},
  doi       = {10.1016/j.jim.2014.07.004},
  pages     = {45 -- 56},
  year      = {2014},
  abstract  = {A novel method that optimizes the screening for antibody-secreting hapten-specific hybridoma cells by using flow cytometry is described. Cell clones specific for five different haptens were analyzed. We selectively double stained and analyzed fixed hybridoma cells with fluorophore-labeled haptens to demonstrate the target-selectivity, and with a fluorophore-labeled anti-mouse IgG antibody to characterize the level of surface expression of membrane-bound IgGs. ELISA measurements with the supernatants of the individual hybridoma clones revealed that antibodies from those cells, which showed the highest fluorescence intensities in the flow cytometric analysis, also displayed the highest affinities for the target antigens. The fluorescence intensity of antibody-producing cells corresponded well with the produced antibodies' affinities toward their respective antigens. Immunohistochemical staining verified the successful double labeling of the cells. Our method makes it possible to perform a high-throughput screening for hybridoma cells, which have both an adequate IgG production rate and a high target affinity. (C) 2014 Elsevier B.V. All rights reserved.},
  language  = {en}
}