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  • 1995-1999  (3)
  • 1990-1994
  • 1900-1904
  • 1999  (3)
  • EP24.15  (2)
  • Brassica campestris  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Antibodies to flowering-plant sperm (1999)
    Springer
    Protoplasma 208 (1999), S. 115-122 
    Details
    ISSN: 1615-6102
    Keywords: Brassica campestris ; Fertilization ; Generative cell ; Monoclonal antibodies ; Sperm
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The mechanisms by which sperm cells recognize and fuse with the egg and central cell during double fertilization in flowering plants are unknown. To identify membrane surface molecules that might function in fertilization, we immunized mice with isolated sperm ofBrassica campestris and screened the polyclonal sera and monoclonal hybridoma supernatants by immunocytochemistry for binding to isolated sperm cells. We identified three cell lines producing hybridoma supernatants which bind to sperm cell surfaces inB. campestris and further analyzed the properties of one of these, BRSP1. The molecular mass of the epitope to BRSP1 was 54 kDa, and was not glycosylated. Although the antibodies were immunoglobulin M, neither removal of carbohydrates nor competition with antibodies which recognize arabinogalactan decreased binding. BRSP1 recognized sperm ofPlumbago zeylanica, Nicotiana tabacum. Arabidopsis thaliana, andEruca vesicaria and generative cells ofLilium longiflorum and ofNarcissus tazetta but did not recognize sperm ofHelianthus annuus, Gerbera jamesonii, orZea mays. Antibodies to plant sperm allow us to probe sperm membranes for functional components.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01279081
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Conformational analysis of an EP24.15 inhibitor by NMR and molecular modelling (1999)
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 395-402 
    Details
    ISSN: 1573-3904
    Keywords: cFP ; conformational analysis ; dynamics simulations ; EP24.15 ; ROESY ; thimet oligopeptidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary The enzyme thimet oligopeptidase (EC3.4.24.15, EP24.15) is responsible for the hydrolysis of a number of neuropeptides. Despite much research examining its substrate specificity, little is known about the conformational requirements of its active site. We have used 1D1H and 2D TOCSY NMR experiments to assign the proton resonances of the EP24.15 inhibitor,N-[1-(R, S)-carboxy-3-phenylpropyl]-Ala-Ala-Tyr-p-aminobenzoate (cFP), and 2D ROESY NMR to investigate whether cFP exhibits any conformational preferences in CD3OD and in aqueous CD3OD. Molecular modelling of charged cFP in the gaseous phase generated a number of conformations that were consistent with the NMR data obtained in CD3OD. Analogous modelling on the uncharged cFP did not result in conformations consistent with any of the NMR data, but did suggest that, under non-polar conditions, cFP could adopt a hairpin conformation which would allow simultaneous coordination of the two carboxyl groups of cFP to the zinc ion in the active site of EP24.15.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02443437
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Conformational analysis of an EP24.15 inhibitor by NMR and molecular modelling (1999)
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 395-402 
    Details
    ISSN: 1573-3904
    Keywords: cFP ; conformational analysis ; dynamicssimulations ; EP24.15 ; ROESY ; thimet oligopeptidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The enzyme thimet oligopeptidase (EC3.4.24.15, EP24.15) is responsible for the hydrolysis of a number of neuropeptides. Despite much research examining its substrate specificity, little is known about the conformational requirements of its active site. We have used 1D 1H and 2D TOCSY NMR experiments to assign the proton resonances of the EP24.15 inhibitor, N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-Tyr-p-aminobenzoate (cFP), and 2D ROESY NMR to investigate whether cFP exhibits any conformational preferences in CD3OD and in aqueous CD3OD. Molecular modelling of charged cFP in the gaseous phase generated a number of conformations that were consistent with the NMR data obtained in CD3OD. Analogous modelling on the uncharged cFP did not result in conformations consistent with any of the NMR data, but did suggest that, under non-polar conditions, cFP could adopt a hairpin conformation which would allow simultaneous coordination of the two carboxyl groups of cFP to the zinc ion in the active site of EP24.15.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008946222327
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
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