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  • 1
    Electronic Resource
    Electronic Resource
    Interaction of monoclonal antibodies with the IgE-receptor on rat mast cells and rat basophilic leukemia (RBL) cells (1986)
    Springer
    Inflammation research 17 (1986), S. 418-426 
    Details
    ISSN: 1420-908X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The close relation between rat mast cells and rat basophilic leukemia (RBL) cells with regard to the presence of receptors for IgE and Fcγ led us to generate monoclonal antobodies directed against cell surface antigens. Hybridomas were obtained by the fusion of NS1 mouse myeloma cells with murine spleen and lymph node cells. The culture supernatants were assayed by two ELISA techniques: a) for the production of mouse immunoglobulin in general and b) for antibodies directed against surface antigens of RBL cells. For this purpose RBL cells were attached to polyvinyl chloride microtitre plates. Eight hybrids produced antibodies directed against surface antigens on RBL cells. Hybrids were cloned and characterized with regard to their isotype and light chains. All eight clones secreted IgM with K light chains. Immunofluorescence studies performed with RBL cells revealed that all eight antibodies were able to show a specific fluorescence. Furthermore, four of these eight antibodies also showed a specific fluorescence with purified rat mast cells. These four antibodies were analyzed as to their ability of interacting with the IgE-receptor on RBL cells and purified rat mast cells. They reduced the binding rate of radiolabelled rat IgE to RBL and rat mast cells. A mutual inhibition of the passive cutaneous anaphylaxis (PCA) reaction in the rat by either mixing mouse reaginic serum directed against 2,4-dinitrophenol bovine serum albumin (DNP-BSA) or by mixing monoclonal mouse anti-DNP IgE with the monoclonal mouse anti-cell surface (rat basophilic leukemia, rat mast cell) IgM was determined. The histamine release of rat mast cells obtained from Nippo-strongylus brasiliensis infected rats was markedly reduced in the presence of two monoclonal anti cell surface antibodies. Our data suggest that monoclonal antibodies with specificity for the IgE receptor (inhibition of IgE-binding) can be distinguished from those which bind closely to the IgE-receptor but also modulate the histamine release from presensitized mast cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01965508
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  • 2
    Electronic Resource
    Electronic Resource
    Ground state properties of UNi"2Al"3 and UPd"2Al"3
    Amsterdam : Elsevier
    Physica B: Physics of Condensed Matter 186-188 (1993), S. 188-194 
    Details
    ISSN: 0921-4526
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0921-4526(93)90531-A
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  • 3
    Electronic Resource
    Electronic Resource
    Solid-state photoreactivity of ortho-distyrylaromatic compounds
    Amsterdam : Elsevier
    Tetrahedron Letters 33 (1992), S. 2795-2798 
    Details
    ISSN: 0040-4039
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/S0040-4039(00)78860-5
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  • 4
    Electronic Resource
    Electronic Resource
    Responses to different external light rhythms by the circadian rhythm of Crassulacean acid metabolism in Kalanchoe daigremontiana (2001)
    Oxford, UK : Blackwell Science Ltd
    Plant, cell & environment 24 (2001), S. 0 
    Details
    ISSN: 1365-3040
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Time series of net CO2 exchange (JCO2) and leaf conductivity for water vapour (gH2O) were measured and subsequently analysed mathematically in the Crassulacean acid metabolism (CAM) plant Kalanchoe daigremontiana (Hamet et Perrier de la Bâthie) under constant environmental conditions and under imposed external rhythms of lower and higher light intensity. The time series were analysed by Fourier methods and a correlation analysis considering the first time derivatives of JCO2, gH2Oand photosynthetically active photon flux density (PPFD). The ratio of internal to external CO2 (ci/ca) was also considered in the analysis, leading to a discussion of the interaction of stomata and carbon assimilation under periodic stimulation. It is suggested that for stimulation with frequencies close to the endogeneous circadian period, stomatal conductance and carbon assimilation oscillate synchronously, guard-cell movements trailing behind changes in internal CO2 with a delay of 10–15 min. For stimulation frequencies far shorter than the endogeneous period, this synchrony can be disturbed due to independent responses of stomata and assimilation to light pulses, leading to an arrhythmic gas exchange pattern. These results are discussed in the context of understanding circadian oscillations as the output of a multioscillator, multisignalling pathway system on the organismic and metabolic level.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.0016-8025.2001.00732.x
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  • 5
    Electronic Resource
    Electronic Resource
    Determination of α"s from energy-energy correlations measured on the Z^0 resonance
    Amsterdam : Elsevier
    Physics Letters B 257 (1991), S. 469-478 
    Details
    ISSN: 0370-2693
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0370-2693(91)91925-L
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  • 6
    Electronic Resource
    Electronic Resource
    Monoclonal murine anti-DNP IgE:in vitro histamine release of rat mast cells in the presence of reaginic rat and mouse sera (1985)
    Springer
    Inflammation research 16 (1985), S. 485-490 
    Details
    ISSN: 1420-908X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Mast cells from normal rats and animals reinfected withNippostrongylus brasiliensis (N.b.) were sensitizedin vitro with monoclonal anti-DNP mouse IgE, reaginic mouse serum with ovalbumin (OA) specificity and reaginic rat serum against N.b. The sensitized cells were triggered for the release of histamine with DNP-bovine-serum-albumin (DNP-BSA), OA, N.b.-homogenate and guinea-pig antimouse IgE. The histamine release from normal mast cells sensitized with monoclonal mouse IgE was inhibited either with N.b.-reaginic rat serum or OA-reaginic mouse IgE (30μg/105 mast cells) completely densensitized mast cells from reinfected rats for specific histamine release in the presence of either N.b.-antigen or DNP-BSA. Anti-mouse IgE which was prepared by monoclonal mouse IgE did not bind to rat mast cells sensitized with rat IgE as was revealed by immunofluorescence experiments. Consequently we observed that anti-mouse IgE failed to trigger the histamine release from mast cells of reinfected rats.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01983651
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  • 7
    Electronic Resource
    Electronic Resource
    Proteins ofNippostrongylus brasiliensis analyzed by immunoblotting (1989)
    Springer
    Parasitology research 75 (1989), S. 482-487 
    Details
    ISSN: 1432-1955
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Antigenic proteins were characterized by the immunoblotting technique with sera from rats and mice after infection as well as hyperimmune sera. The immune response of infected animals was mainly directed toward five proteins of adult worms (190, 118, 110, 98, and 52 kDa) and four proteins of the third larval stage (L3; 92, 78, 58, and 24 kDa). The immunoblots indicated that stage-specific proteins of the homogeneates were recognized. Three stage-specific proteins of L3 larvae (150, 135, and 125 kDa) and three proteins typical to the adult worm (100, 82, and 67 kDa) were identified. The majority of the worm proteins elicited an IgG response. IgE synthesis was induced by living and dead parasites and was directed towards four proteins (190, 150, 125, and 98 kDa). Three proteins additionally induced an IgG or IgM antibody response. The immune response as shown by the immunoblotting technique seems to be directed towards (1) antigens that are present for the duration of an infection and (2) stage-specific antigens that are expressed for only a short time during the life cycle of the parasite.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00930977
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  • 8
    Electronic Resource
    Electronic Resource
    IgE synthesis in vitro during infection of mice with the nematodeNippostrongylus brasiliensis: Effects of mitogens and antigens (1985)
    Springer
    Parasitology research 71 (1985), S. 649-662 
    Details
    ISSN: 1432-1955
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract In vitro IgE synthesis by lymphoid cells was studied during the course of infection of mice withNippostrongylus brasiliensis. The studies involved inbred strains of mice which had been shown to be high IgE responders (A.CA, B10.M), or non-responders (Balb/c, B10.D2) to parasite antigen. In addition, F1 hybrids of low and high responders and irradiated non-responders were studied. Infection withN. brasiliensis led to an increase in IgE synthesis in vitro which was most pronounced during reinfection of mice. Addition of mitogens e.g. pokeweed mitogen (PWM), lipopolysaccharide (LPS), concanavalin A (ConA) to the cultures induced enhancement, suppression or had no effect on IgE synthesis. Addition ofN. brasiliensis homogenate or worm culture supernatant led to a fluctuating pattern of IgE synthesis. No correlation was found between lymphocyte proliferative response to mitogen and worm antigens and IgE synthesis. Our data suggest, that PWM is more likely to enhance IgE synthesis in vitro than LPS or ConA. An enhancement is more easily observed with the cells of non-infected animals or during the early phase of infection or reinfection. The mitogen-induced increase in IgE synthesis did not exceed the values obtained during infection or reinfection.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00925598
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  • 9
    Electronic Resource
    Electronic Resource
    Characterization of antigens of the nematodeNippostrongylus brasiliensis by monoclonal antibodies (1985)
    Springer
    Parasitology research 71 (1985), S. 663-672 
    Details
    ISSN: 1432-1955
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Hybridomas secreting monoclonal antibodies toNippostrongylus brasiliensis antigens were generated by hybridization of IR983F myeloma cells with spleen cells from Lou/M/Wol rats infected with living third-stage larvae. Antibodies specific either for larval or worm antigens were identified by enzyme-linked immunosorbent assays withNippostronylus brasiliensis fragments, homogenates and secretions as antigens. The results demonstrate that all antibodies which recognized larval antigens (38 antibodies) also reacted with worm surfaces. Ten antibodies were specific only for worm antigens. Ten antibodies reacted with worm homogenate, three antibodies recognized components of worm secretion and 17 antibodies combined with acetylcholinesterase. The epitope specificity was investigated by the capacity of various glycosides, aminoacids,N-acetylneuraminic acid and phosphorylcholine to inhibit the binding to worm fragments. The analysis revealed that α-methylglucoside, α-methylmannoside,N-acetylglucosamine,N-acetylgalactosamine, fucose and the amino acids leucine, phenylalanine, tyrosine, serine, tryptophan did not combine with the antigen-binding sites of the antibodies. Proline, arginine and histidine, however, displayed inhibitory effects. WithN-acetylneuraminic acid as inhibitor three groups of antibodies could be discriminated. At a concentration of 10–20 mM, phosphorylcholine was a potent inhibitor for all antibodies.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00925599
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