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  • Articles: DFG German National Licenses  (4)
  • 1990-1994  (4)
  • 1980-1984
  • Acinetobacter baumannii  (2)
  • serology  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 162 (1994), S. 249-254 
    ISSN: 1432-072X
    Keywords: Key words     Siderophore ; Iron-uptake ; Acinetobacter baumannii ; Acinetobactin ; ω-N-Hydroxyhistamine ; 2 ; 3-Dihydroxybenzoic acid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract      A novel siderophore, called acinetobactin, with both catecholate and hydroxamate functional groups was isolated from low-iron cultures of Acinetobacter baumannii ATCC 19606. The structure was elucidated by chemical degradation, fast-atom bombardment mass spectrometry and 1H and 13C NMR spectroscopy. Acinetobactin was composed of ω-N-hydroxyhistamine, threonine and 2,3-dihydr ybenzoic acid, the last two components forming an oxazoline ring. Acinetobactin was structurally related to anguibactin, a plasmid-encoded siderophore of Vibrio anguillarum. The only difference was that acinetobactin possessed an oxazoline ring instead of a thiazoline ring. Four of 12 other clinical A. baumannii strains examined produced acinetobactin, indicative of strain-to-strain variation in the ability to produce acinetobactin. In addition, a relatively small amount of acinetobactin w as also detected in A. haemolyticus ATCC 17906.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 162 (1994), S. 249-254 
    ISSN: 1432-072X
    Keywords: Siderophore ; Iron-uptake ; Acinetobacter baumannii ; Acinetobactin ; ω-N-Hydroxyhistamine 2,3-Dihydroxybenzoic acid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A novel siderophore, called acinetobactin, with both catecholate and hydroxamate functional groups was isolated from low-iron cultures of Acinetobacter baumannii ATCC 19606. The structure was elucidated by chemical degradation, fast-atom bombardment mass spectrometry and 1H and 13C NMR spectroscopy. Acinetobactin was composed of ω-N-hydroxyhistamine, threonine and 2,3-dihydroxybenzoic acid, the last two components forming an oxazoline ring. Acinetobactin was structurally related to anguibactin, a plasmid-encoded siderophore of Vibrio anguillarum. The only difference was that acinetobactin possessed an oxazoline ring instead of a thiazoline ring. Four of 12 other clinical A. baumannii strains examined produced acinetobactin, indicative of strain-to-strain variation in the ability to produce acinetobactin. In addition, a relatively small amount of acinetobactin was also detected in A. haemolyticus ATCC 17906.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Veterinary research communications 16 (1992), S. 185-193 
    ISSN: 1573-7446
    Keywords: anti-immunoglobulin ; chicken ; enhancement ; haemagglutination inhibition ; Mycoplasma gallisepticum ; serology
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Addition of anti-immunoglobulin M (anti-IgM), G (anti-IgG) and A (anti-IgA) sera to the haemagglutination-inhibition (HI) test (anti-Ig HI test) forMycoplasma gallisepticum resulted in 2- to 8-fold increases in the HI titres. On investigating the anti-Ig HI reaction using IgM and IgG antibodies separated by affinity chromatography, it was confirmed that, in the enhanced HI titres, specificity existed between the chicken Ig classes having antibody activity and the antisera used in the test. Four days after inoculation ofM. gallisepticum, the anti-Ig HI reaction was markedly enhanced by anti-IgM antiserum in the intravenously inoculated chickens and by anti-IgA serum in the nasally inoculated chickens. Ten days after inoculation ofM. gallisepticum marked enhancement of the reaction was produced by anti-IgG serum in both intravenously and nasally inoculated chickens, but the enhancement of the anti-Ig HI reaction diminished from the second week after inoculation.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Veterinary research communications 17 (1993), S. 259-266 
    ISSN: 1573-7446
    Keywords: antigen ; C-reactive protein ; dog ; epitopes ; immunoelectrophoresis ; human ; serology ; Western blot
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Differences in antigenicity between human and canine C-reactive proteins were investigated by Western blotting analysis. It was confirmed that several commercial anti-human CRP sera reacted with canine CRP. However, 34 anti-canine CRP sera prepared by immunization of rabbits and goats with canine CRP all reacted with canine CRP but not with human CRP in either immunoelectrophoresis or Western blotting. Immunization with human CRP produced a cross-reacting antibody that reacted with canine CRP. Conversely, immunization with canine CRP did not produce a cross-reacting antibody that reacted with human CRP. These findings may be interpreted as showing that, while canine and human CRPs do not share common antigenicity, they do contain structurally similar antigenic determinants.
    Type of Medium: Electronic Resource
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