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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 8 (1993), S. 0 
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 22 (1985), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The specificity of monoclonal antibodies against Mycobacterium tuberculosis was determined by crossed immunoelectrophoresis, Radiolabelled, non-precipitating monoclonal antibody was incorporated in the top gel together with unlabelled polyvalent, precipitating anti-bacillus Calmette-Guérin (BCG) antibody. Inclusion of labelled antibody in individual precipitate fines was demonstrated by autoradiography. Each monoclonal antibody was localized in a single precipitate line: antibody TB73 reacted with BCG antigen 56: TB71 and TB72 reacted with BCG antigen 78: and TB78 reacted with BCG antigen 82. The technique permits precise determination of the specificity of monoclonal antibodies at the level of reactivity with native immunogenic components of complex microorganisms without prior antigen purification.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 34 (1991), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: A set of seven murine monoclonal antibodies were generated against a chemically synthesized 11-kDa 104-mer peptide covering the C-terminal residues 270-373 of the p24g.it; protein (HIV-IBRU strain). All monoclonal antibodies recognized HIV-LMN infected MOLT? cells by fluorescence und gave positive Western blot signals with viral gag peptides [p55 and/or p24), Oligopeptide binding regions were located with competitive enzyme-linked immunosorbent assays. Detailed epitope scanning analyses (the Geysen technique) were performed by serological testing of the monoclonal antibodies against 99 overlapping hexapeptides which corresponded to the entire 104-mer region. The antibodies bound to p24 peptide sequences located within the 275 2y3 and 351 36S regions. One antibody (LH 104-B) which reacted with residues 357-362 bound lo p55 alone. In contrast another antibody (LH 104–1). which recognized the residues 358–363. i.e. with five out of six residues in common with antibody LIIKM-B for its epitope region, reacted exclusively with p24.At least two of the antibodies (LH104-C and -A) which bound to p24 alone, apparently recognized conformational epitopes, They gave positive reactions with the regions 288—293/351–356 and 284–289/351–356, respectively.This work shows that chemical synthesis of large peptides is a viable alternative approach to immunochemical studies of viral proteins.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 31 (1990), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: We have previously demonstrated the pathogenicity of the common anti-DNA idiotype designated 16/6 Id. Immunization of naive mice with the 16/6 Id induced SLE-like disease characterized by serological (e.g. anti-dsDNA and anti-Sm auto-antibodies), clinical (increased ESR, leucopenia and proteinuria), and pathological (16/6 Id deposition in kidneys) parameters. To elucidate further the role of the 16/6 Id in SLE induction the following studies were carried out: BALB/c mice were immunized with SA-1, a human anti-DNA monoclonal antibody carrying the 16/6 Id; TB-68, a mouse monoclonal anti-tuberculosis (TB) glycolipid, which binds dsDNA and carries the 16/6 Id; TB-72, a mouse monoclonal anti-TB glycolipid that binds DNA and does not harbour the 16/6 Id; and 4B4, a human anti-Sm antibody that carries the 16/6 Id. SLE was induced in BALB/c mice only when immunized with SA-l, TB-68, and 4B4, namely antibodies with diverse binding capacities albeit having the 16/6 Id. Our studies further support previous evidence on the pathogenic role attributed to the 16/6 Id in SLE, and suggest that SLE is most probably an idiotype-induced disease.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Inflammation research 45 (1996), S. 155-158 
    ISSN: 1420-908X
    Keywords: Molecular chaperones ; Therapy ; Heatshock proteins disease ; Cytokines
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Molecular chaperones are intracellular proteinfolding proteins which form part of an ancient cellular response to stress called the heat shock response. They have been the focus for attention during the last decade because of the discovery of their vital role in cell functioning. In very recent years additional roles for these ‘topologically-active’ proteins in the process of tissue pathology and its treatment have been indicated and are reviewed.
    Type of Medium: Electronic Resource
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