Zobrazeno 1 - 10
of 47
pro vyhledávání: '"J N, Limet"'
Autor:
Jean-Jacques Letesson, T. K. O. Vo, J. N. Limet, Michel S. Zygmunt, Dominique Gilson, Philippe Denoel, Anne Tibor, Vincent Weynants
Publikováno v:
University of Namur
Brucellergene is a commercial allergen prepared from Brucella melitensis strain B115 and containing at least 20 cytoplasmic proteins. These proteins were separated by SDS-PAGE. The unstained gel was divided into 18 fractions and proteins were eluted
Publikováno v:
University of Namur
Infection and Immunity
Infection and Immunity, American Society for Microbiology, 1996, 64 (1), pp.100-107
Infection and Immunity
Infection and Immunity, American Society for Microbiology, 1996, 64 (1), pp.100-107
Screening of a Brucella abortus genomic library with two sets of monoclonal antibodies allowed the isolation of the genes corresponding to two minor outer membrane proteins (OMP10 and OMP19) found in this bacterial species. Sequence analysis of the o
Publikováno v:
Journal of Bacteriology
Journal of Bacteriology, American Society for Microbiology, 1995, 177 (7), pp.1911-1914
Journal of Bacteriology, American Society for Microbiology, 1995, 177 (7), pp.1911-1914
The cloning and sequencing of the Brucella abortus major 25-kDa outer membrane protein (OMP) is reported. The 25-kDa (group 3) OMP has been proposed, on the basis of amino acid composition, to be the counterpart of OmpA (D. R. Verstraete, M. T. Creas
Publikováno v:
Journal of Medical Microbiology. 39:403-407
The antibody response of cattle to the minor 89-kDa outer-membrane protein (OMP) of brucella was measured by indirect ELISA with the purified protein and compared with the antibody response to smooth lipopolysaccharide (S-LPS). Pre-incubating sera wi
Publikováno v:
Research in Microbiology. 144:475-484
We characterized 4 monoclonal antibodies (mAb) specific for rough lipopolysaccharide (R-LPS) of Brucella. mAb were selected by enzyme-linked immunosorbent assay (ELISA) on whole B. abortus 45/20 rough cells and R-LPS from B. melitensis B115 rough cel
Publikováno v:
Journal of Immunological Methods. 131:137-142
We describe here two latex immunoassays for total thyroxine (T4) and total triiodothyronine (T3). These homogeneous 60 min assays are quantified by optically counting the monomeric particles remaining after agglutination. When precision is assessed,
Autor:
Jacques Godfroid, Gérard Dubray, D. Gilson, L. De Waele, J. N. Limet, P. Flanagan, T. K. O. Vo, Jean-Jacques Letesson, Claude Saegerman, A. Bastin
Publikováno v:
The Veterinary record. 145(8)
Brucellergene OCB (Rhone-Merieux) was used as an allergen to define the intrinsic parameters of a skin test and to compare its properties with serology for the diagnosis of bovine brucellosis. The skin test was also evaluated for its capacity to solv
Autor:
Jean-Jacques Letesson, D. Gilson, Vincent Weynants, A Cloeckaert, Philippe Denoel, Fabrice Godfroid, Anne Tibor, J. N. Limet
Previously, four epitope specificities on the O chain of Brucella species were reported: M, A, C, and C/Y. In this work, according to monoclonal antibody binding to smooth lipopolysaccharides of Yersinia enterocolitica 0:9, Brucella abortus W99 (A-do
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7543e6be42a751b6cf63c4c4e3312e8f
https://europepmc.org/articles/PMC175246/
https://europepmc.org/articles/PMC175246/
Autor:
A Cloeckaert, Jean-Jacques Letesson, J. N. Limet, Anne Tibor, Philippe Denoel, P. Thiange, Vincent Weynants, D. Gilson
Publikováno v:
University of Namur
The reactivity of monoclonal antibody (MAb) 12G12 was analyzed in regard to the main biovars of Brucella species and some members of the families Enterobacteriaceae and Vibrionaceae which present serological cross-reactions with the smooth lipopolysa
Autor:
Bernadette Lichtfouse, J. N. Limet, Pascal Briffeuil, Philippe Denoel, Anne Tibor, Vincent Weynants, Jean-Jacques Letesson, Michel S. Zygmunt
Publikováno v:
University of Namur
The 40 N-terminal amino acids of the 20 kDa antigen A2 from Brucella melitensis were sequenced and showed important similarities with 4 bacterioferritins. A monoclonal antibody raised against this antigen cross-reacted with Escherichia coli bacteriof