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  • 2005-2009
  • 1990-1994  (3)
  • Acinetobactin  (2)
  • HMM decoration  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Isolation and structure elucidation of acinetobactin, a novel siderophore from Acinetobacter baumannii (1994)
    Springer
    Archives of microbiology 162 (1994), S. 249-254 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00301846
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Isolation and structure elucidation of acinetobactin., a novel siderophore from Acinetobacter baumannii (1994)
    Springer
    Archives of microbiology 162 (1994), S. 249-254 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00301846
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Dense bands and polarity of thin filament at myotendinous junction in guppy muscle (1990)
    Springer
    Protoplasma 158 (1990), S. 121-129 
    Details
    ISSN: 1615-6102
    Keywords: Myotendinous junction ; Dense bands ; Lebistes reticulates ; Myomyous junction ; HMM decoration ; Ca2+-activated protease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Guppy muscle shows unique electron dense bands in the terminal segment of the myofibril at the muscle—tendon junction. On occasion electron dense bands were also observed at the myomyous junction. The unusual bands are approximately 70 nm wide with an electron density similar to that of Z-lines. Thin filaments seem to be continuous throughout these dense bands with no interdigitation of filaments before the membrane. Calcium-activated neutral protease removes the dense bands. The filaments of the terminal segment are decorated by heavy meromyosin and therefore are actin. The polarity of actin filaments, determined by the arrowhead pattern formed when the filaments are decorated with HMM, appears to be directed away from the sarcolemma. No evidence of polarity reversal was observed at the dense bands. Although function and significance is unknown, we assume the electron dense bands of the myofibril terminal segment of guppy muscle are not Z-lines, but rather, are structures unique to guppy muscle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01323124
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
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