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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Plant, cell & environment 11 (1988), S. 0 
    ISSN: 1365-3040
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Two monoclonal antibodies (AFRC MAC 184 and 185) have been raised in rats against a synthetic octadecapeptide corresponding to the N-terminus of Avena phytochrome. The peptide was conjugated to tuberculin purified protein derivative (PPD) for immunization and the cell lines screened by ELISA using the free peptide. Both antibodies bind to intact 124-kDa phytochrome on Western blots and in a double antibody sandwich ELISA. In the ELISA, they have an approximately four-fold higher affinity for Pr than Pfr. Conformational changes during photoconversion, therefore, involve the extreme N-terminus of the phytochrome molecule.
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 14 (1987), S. 0 
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Astrocytes, astrocytic cell lines and endothelium from BDIX rats were stimulated with recombinant interferon-gamma (IFN-γ) and the expression of MHC molecules quantified using an enzyme immunoassay (EIA). Using the two mouse anti-RT1.B monoclonal antibodies MRC OX4 and OX6, previously described as recognizing a monomorphic determinant on RT1.B, as well as polyvalent rabbit anti-rat class II antisera, we were unable to demonstrate any induction of RT1.B molecules on these cells under conditions that induced RT1.B expression in all other strains tested. In contrast, RT1.D locus class II molecules, detectable by the antibody MRC OX17, are more strongly expressed in BDIX than in other strains. In experiments using BDIX lymphocytes, this serologically detected defect in RT.1B expression was confirmed using four additional mouse anti-mouse I-Ak monoclonal antibodies, which cross-reacted on all rat strains tested except BDIX. It appears likely that BDIX rats lack either a structural or controlling gene required for RT1.B expression.
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 12 (1985), S. 0 
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The rat CT antigens are a system of medial histocompatibility antigens linked to RT1, the rat major histocompatibility complex (MHC). They have aroused interest firstly because, despite their extreme serological weakness, they are targets for ‘unrestricted’ cytotoxic T lymphocytes (CTL); and secondly because they have appeared to represent a complex genetic system in terms both of the number of genetic loci involved and the number of distinguishable antigenic specificities expressed. The CT system was originally defined by the reactions of LEW anti-F344 (RT1l anti-RT1lvl) secondary in vitro CTL. These CTL reacted strongly on DA(RT1avl) targets, but much more weakly on AUG or PVG (RT1c) targets. We have used the recently derived RT1 recombinant rat strains PVG.R19 (RT1.AavlIavlCc) and PVG.R20 (RT1.AcIcCavl) to investigate the genetic control of this system. Contrary to previous interpretations, the results are consistent with a model in which CT is a single locus, which maps to the RTI.C region. In addition, our results demonstrate that there is cross-reactivity of anti-RT1C CTLs on RT1A products, and we suggest that the earlier placement of a CT locus in the RT1.A region was probably incorrect and a consequence of this cross-reactivity.
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  • 4
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 266 (1977), S. 550-552 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] We report here the derivation of lines of hybrid cells secreting antibody to rat major histocompatibility antigens. The hybrids were made by fusion of a mouse myeloma cell line1, P3-X63-Ag8, with spleen cells of AO strain rats immunised against DA strain antigens. In previous experiments we used ...
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 13 (1986), S. 0 
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Polyvalent alloantisera, prepared by reciprocal immunization of F344 (RT1lv1 haplotypes) and WF (RT1u haplotype) rats, as well as monoclonal antibodies, were used to immunoprecipitate class I alloantigens from detergent extracts of monolayer cultures of 35S-methionine-labelled liver cells. Two-dimensional IEF/SDS-PAGE gel analysis resolved the RT1.Alv1 and RT1.Au class I antigens expressed on the liver cells in culture.
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  • 6
    ISSN: 1432-2048
    Keywords: Avena (phytochrome) ; Immunological discrimination ; Monoclonal antibody ; Phytochrome (red-, far-red absorbing forms)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A set of rat monoclonal antibodies (ARC MAC 48 to 52 and 54 to 56), raised to phytochrome from dark-grown seedlings of Avena sativa L. was tested for the ability to discriminate between the red-absorbing (Pr) and far-red-absorbing (Pfr) forms of phytochrome by indirect enzyme-linked immunosorbent assay. MAC 50 bound more strongly to Pfr and MAC 49 and 52 showed preferential binding to Pr from extracts of dark-grown Avena seedlings; MAC 50 also bound more strongly to Pfr from brushite-purified phytochrome. The remainder of the monoclonal antibodies and a rabbit polyclonal antiphytochrome preparation did not discriminate between Pr and Pfr. The results provide evidence for conformational changes in defined regions of the phytochrome apoprotein upon photoconversion.
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  • 7
    ISSN: 1573-4927
    Keywords: mouse sucrase ; regulatory gene ; disaccharidases
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Assays for sucrase carried out on intestinal sonicates prepared from 18 different strains of mice revealed a threefold variation in specific activity, the values for CBA/Ca mice being significantly less than for any other strain. Further comparison of the CBA/Ca versus the C57BL/6J mouse showed this deficiency, which became established 2–4 weeks after birth, to apply to isomaltase as well as sucrase but not to maltase or trehalase. Backcross experiments indicated that this deficiency in sucrase activity was inherited as a single codominantly expressed genetic factor. The ability of the CBA/Ca mouse to regulate sucrase activity in response to changes in diet was also reduced compared to that of the C57BL/6J mouse. No difference could be detected in the affinity of sucrase for its substrate or in the ability of heat to denature sucrase prepared from CBA/Ca and C57BL/6J mice. It is suggested that part of the regulatory region of the gene coding for sucrase-isomaltase is modified in the CBA/Ca mouse and that this locus should be given the notation Suc-1 for future reference.
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  • 8
    ISSN: 1432-2048
    Keywords: Gibberellin (monoclonal antibodies, structure specificity) ; Immunoassay ; Monoclonal antibody
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The production and characterization of high-affinity monoclonal antibodies (McAb) to gibberellins (GAs) is reported. Hybrid myelomas were derived from immunisations with conjugates in which immunogenic proteins were linked to GA1 at carbon-3 and to GA4 and GA9 at carbon-17. A series of McAb which display specificities allowing recognition of, and the discrimination between GA1, GA20, GA4 and GA9 is described. These McAb can be used in quantitative immunoassays for underivatised GAs.
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  • 9
    ISSN: 1432-2048
    Keywords: Glycoprotein ; Infection thread matrix glycoprotein ; Lipopolysaccharide ; Monoclonal antibody ; Pisum (root nodule) ; Plasma membrane glycoprotein ; Rhizobium ; Root nodule
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Plant and bacterial antigens contributing to nodule development and symbiosis in pea (Pisum sativum L.) roots were identified after isolation of a set of monoclonal antibody (McAb)-producing hybridoma lines. Rats were immunised with the peribacteriod material released by mild osmotic shock treatment from membrane-enclosed bacteroids of Rhizobium leguminosarum bv. viceae. In order to diversify the range of McAb specificities, this material was either used as immunogen directly (method 1), or after immunodepletion of a set of glycoprotein and lipopolysaccharide antigens (method 2), or after deglycosylation (method 3). After fusion and screening of cloned hybridoma lines, these three immunisation methods gave respectively 4, 2 and 1 classes of McAb with unique antigen specificities. Ultrastructural immunogold localisation studies showed four different antigens to be present on peribacteriod and plasma membranes (identified by MAC 64, 202, 206 or 209); in addition, a glycoprotein of plant origin but present in the infection-thread matrix was identified by MAC 204. Although none of the epitopes recognised by these McAb was nodule-specific, several were found to be more abundant in extracts of nodule tissue than in uninfected roots (MAC 64, 202, 204, 206). Two McAb reacted with new bacterial antigens: MAC 203 identified a bacterial antigen expressed upon infection but not in free-living cultures of Rhizobium, and MAC 115 identified a bacterial polypeptide (55 kdaltons) that was present in both free-living and bacteroid forms. There were also some McAb of broader specificity that react with antigens present in both plant and bacterial cytoplasms.
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  • 10
    ISSN: 1432-2048
    Keywords: Light and plant growth ; Photoperiodism ; Phytochrome (type 1) ; Triticum (phytochrome)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The kinetics of type 1 phytochrome were investigated in green, light-grown wheat. Phytochrome was measured by a quantitative sandwich enzyme-linked immunosorbent assay using monoclonal antibodies. The assay was capable of detecting down to 150 pg of phytochrome. In red light, rapid first-order destruction of the far-red-light-absorbing form of phytochrome (Pfr) with a half-life of 15 min was observed. Following white light terminated by red, phytochrome synthesis was delayed in darkness by about 15 h compared to plants given a terminal far-red treatment. Synthesis of the red-light-absorbing form of phytochrome (Pr) was zero-order in these experiments. Phytochrome synthesis in far-red light was approximately equal to synthesis in darkness in wheat although net destruction occurred in light-grown Avena sativa tissues in continuous far-red light, as has been reported for other monocotyledons. In wheat, destruction of Pfr apparently did not occur below a certain threshold level of Pfr or Pfr/total phytochrome. These results are consistent with an involvement of type 1 phytochrome in the photoperiodic control of flowering in wheat and other long-day plants.
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