Zobrazeno 1 - 10
of 44
pro vyhledávání: '"Jan Kolberg"'
Publikováno v:
Hybridoma. 30:1-9
Glycophorins comprise the major sialoglycoproteins of the human erythrocyte membrane. Several years ago we described a murine monoclonal antibody (MAb), designated 124,D-7 (IgM), developed by in vitro immunization with human erythrocyte membranes as
Autor:
Jan Kolberg, Terje E. Michaelsen
Publikováno v:
Acta Pathologica Microbiologica Scandinavica Series C: Immunology. :25-35
Antibodies were made against the two-chain lectin Lath-O from the seeds of Lathyrus odoratus as well as its isolated light (alpha) and heavy (beta) chains. These antibodies were used to antigenically compare the Lath-O with other two-chain lectins li
Autor:
Jan Kolberg, Franco Felici, Peter W. Andrew, Angela Scuderi, Marco R. Oggioni, Carla Lo Passo, Helen Baxendale, David Goldblatt, Claire Smith
Publikováno v:
European Journal of Immunology. 39:1527-1535
Anti-polysaccharide immunity is a key facet of protection against several bacterial pathogens. Problems exist with current polysaccharide vaccines and alternative strategies that deliver a protective response are needed. We have identified immunologi
Publikováno v:
Acta Pharmacologica et Toxicologica. 29:81-86
The effect of 2,4-dichlorophenoxyacetic acid (2,4-D) on L 929 cells in monolayer cultures has been studied. It was found that 2,4-D in the range of 50 to 500 μg/ml had a dose dependent inhibitory effect on cell growth. With 350 and 500 μg/ml comple
Autor:
E. Arne Høiby, Jan Kolberg, Wegene Tamire, Morten Harboe, Degu Berhanu, Yared Merid, Einar Rosenqvist, Getahun Mengistu, Dominique A. Caugant, Afework Kassu, Dereje Fikremariam, Elisabeth Fritzsønn, Torill Tangen, Gunnstein Norheim, Berhanu Melak, Abraham Aseffa, Mohammed A. Yassin
Publikováno v:
Clinical and Vaccine Immunology. 15:863-871
Dissecting the specificities of human antibody responses following disease caused by serogroup A meningococci may be important for the development of improved vaccines. We performed a study of Ethiopian patients during outbreaks in 2002 and 2003. Ser
Autor:
Jan Kolberg, Audun Aase, Ronald Frank, Gunnhild Rødal, Tove Karin Herstad, Sven Hammerschmidt, Manfred Rohde, Simone Bergmann
Publikováno v:
Microbiology. 152:1307-1317
Enolase represents one of the anchorless surface proteins ofStreptococcus pneumoniaeand has previously been identified as a plasminogen-binding protein, endowing this pathogen with host proteolytic activity. In this study the mAb 245,C-6 (IgG1) was p
Publikováno v:
FEMS Immunology & Medical Microbiology. 31:175-180
Immunisation of BALB/c mice with seven heat-treated Norwegian clinical isolates of Streptococcus pneumoniae of different serotypes elicited mainly monoclonal antibodies (mAbs) to pneumococcal surface protein A (PspA). It was remarkable that the fusio
Autor:
G Troncoso, M.T. Criado, Einar Rosenqvist, Carlos M. Ferreirós, Jan Kolberg, Manuel Veiga, Sandra Sánchez
Publikováno v:
FEMS Microbiology Letters. 199:171-176
The RmpM protein has been reported to be present only in pathogenic Neisseria species. In the present study we demonstrate that this protein is also present at least in N. lactamica and N. sicca strains. The N. lactamica protein reacts with a RmpM-sp
Autor:
Jan Tommassen, E. Arne Høiby, Audun Aase, Ellen Namork, Alexei A. Delvig, E Wedege, Terje E. Michaelsen, Alexis Musacchio, Einar Rosenqvist, Rolf Dalseg, Jan Kolberg
Publikováno v:
Infection and Immunity. 67:1267-1276
Antibodies against the class 4 outer membrane protein (OMP) from Neisseria meningitidis have been purified from sera from vaccinees immunized with the Norwegian meningococcal group B outer membrane vesicle vaccine. The human sera and purified antibod
Autor:
L. Oddvar Frøholm, Gunnar Bjune, E. Arne Høiby, Ellen Namork, Dominique A. Caugant, Svein Rune Andersen, Jan Kolberg, Erik Jantzen
Publikováno v:
Microbial Pathogenesis. 23:139-155
We wanted to compare the potential protective capacity of antibodies to meningococcal lipopolysaccharides (LPS). The frequency of occurrence and degree of expression of the epitopes recognized by murine monoclonal antibodies (MAbs) to immunotypes L3,