Browsing by Author "Yurdusev, N."
Now showing 1 - 3 of 3
Results Per Page
Sort Options
Item Open Access Generation of mouse hybridomas secreting anti-salmonella enteritidis antibodies and their preliminary characterization(2011) Büyüktanır, O.; Yaǧcı, Tamer; Findık, A.; Yıldırım, T.; Yurdusev, N.BALB/c mice were intraperitoneally immunized with inactivated bacteria for generation of monoclonal anti-S. Enteritidis antibody. The spleen cells of the highest responder animal at fifth immunization were used as the fusion partner of the mouse Sp2/0 myeloma cells. A total of 6 stable hybridomas secreting IgM and IgG isotype antibodies were obtained. These hybridomas were found to be reactive with three S. Enteritidis antigens having relative molecular weights of 73, 59 and 42kDa in Western blot analysis. The 59kDa molecule corresponds to the flagellin protein. From this preliminary study, it can be concluded that further investigations are necessary to obtain monoclonal hybrid cells secreting monoepitopic and monoisotypic antibody by subcloning of the parental hybridomas.Item Open Access A monoclonal antibody against DNA binding helix of p53 protein(Nature Publishing Group, 2001) Yolcu, E.; Sayan, B. S.; Yağci, T.; Cetin Atalay, R.; Soussi, T.; Yurdusev, N.; Ozturk, M.Three monoclonal antibodies (Mabs) were generated against p53 DNA-binding core domain. When tested by immunoprecipitation, Western blot and immunofluorescence techniques, Mab 9E4, as well as 7D3 and 6B10 reacted with both wild-type and various mutant p53 proteins. The epitopes recognized by Mabs 7D3, 9E4 and 6B10 were located respectively within the amino acid residues 211-220, 281-290 and 291-300 of human p53 protein. The epitope recognized by 9E4 Mab coincides with helix 2, also called p53 DNA binding helix, which allows the direct contact of the protein with its target DNA sequences. This antibody may be useful to study transcription-dependent and transcription-independent activities of wild-type and mutant p53 proteins.Item Open Access A recombinant PvpA protein-based diagnostic prototype for rapid screening of chicken mycoplasma gallisepticum infections(Elsevier, 2008) Büyüktanir, O.; Yildirim, T.; Yakicier, C.; Genç, O.; Yurdusev, N.Mycoplasma gallisepticum is the primary agent of chronic respiratory disease causing important economic losses in the poultry industry. Serological monitoring is essential to maintain mycoplasma-free breeder flocks and often complicated by the cross-reactions between different mycoplasma species. To overcome serological cross-reactions, a large fragment of the M. gallisepticum PvpA cytadhesin, species-specific surface-exposed protein, was produced in E. coli as a recombinant protein (rPvpA336) and used as a potential diagnostic antigen. The rPvpA336 protein possesses 336 mycoplasma-specific amino acids with relative molecular weight of 44 kDa. A deletion region of 37 amino acids was identified when compared to the wild-type PvpA protein. Immunoreactivity of the rPvpA336 protein has been demonstrated by Western blot analysis with M. gallisepticum-positive and -negative chicken sera. Furthermore, an enzymatic rapid immunofiltration assay (ERIFA) prototype based on the rPvpA336 protein has been developed and its species-specific detection capability has been demonstrated by using M. gallisepticum and/or M. synoviae-positive and -negative chicken sera. In addition to its species-specificity, the ERIFA prototype presents certain advantages such as rapidity, field-applicability and cost-effectiveness. Therefore, these advantages would make the prototype a species-specific rapid diagnostic tool of choice in the field and limited laboratory conditions for screening M. gallisepticum infections. © 2007 Elsevier B.V. All rights reserved.