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  • 1
    Electronic Resource
    Electronic Resource
    Effect of iron on expression of superoxide dismutase by Aeromonas salmonicida and associated resistance to superoxide anion (1996)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 142 (1996), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Superoxide dismutase activity was detected in Aeromonas salmonicida under iron-replete and iron-limited culture conditions. Under iron-replete conditions an iron superoxide dismutase, molecular mass 50,400 Da, was identified based on inhibition by hydrogen peroxide but not by millimolar concentrations of cyanide. When the available iron in the culture medium was limited by addition of the non-assimilable iron chelator 2,2-dipyridyl, a manganese superoxide dismutase, molecular mass 45,600 Da, was identified, which was resistant to inhibition by either hydrogen peroxide or cyanide. The change in enzyme production would appear to be iron dependent, as addition of FeCl3 in excess to iron-limited broths resulted in only the iron superoxide dismutase being synthesised. Examination of the location of the superoxide dismutase enzymes revealed that the manganese superoxide dismutase expressed under iron limitation is located in the periplasm, while the iron superoxide dismutase has a cytoplasmic location. The periplasmic manganese superoxide dismutase was able to protect A. salmonicida against extracellular riboflavin-generated superoxide, with A. salmonicida grown under iron-limited conditions exhibiting a 32-fold increase in minimum bactericidal concentration of riboflavin compared to cells cultured under iron-replete conditions. Furthermore, in a time-course study of bactericidal activity of exogenously generated superoxide against A. salmonicida, bacteria grown under iron-replete conditions and expressing cytoplasmic iron superoxide dismutase were rapidly killed, whilst those grown under iron limitation expressing periplasmic manganese superoxide dismutase survived for the duration of the experiment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1996.tb08401.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    AIP56, a novel plasmid-encoded virulence factor of Photobacterium damselae subsp. piscicida with apoptogenic activity against sea bass macrophages and neutrophils (2005)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 58 (2005), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: A strategy used by extracellular pathogens to evade phagocytosis is the utilization of exotoxins that kill host phagocytes. We have recently shown that one major pathogenicity strategy of Photobacterium damselae subsp. piscicida (Phdp), the agent of the widespread fish pasteurellosis, is the induction of extensive apoptosis of sea bass macrophages and neutrophils that results in lysis of these phagocytes by post-apoptotic secondary necrosis. Here we show that this unique process is mediated by a novel plasmid-encoded apoptosis inducing protein of 56 kDa (AIP56), an exotoxin abundantly secreted by all virulent, but not avirulent, Phdp strains tested. AIP56 is related to an unknown protein of the enterohemorrhagic Escherichia coli O157:H7 and NleC, a Citrobacter rodentium type III secreted effector of unknown function. Passive immunization of sea bass with a rabbit anti-AIP56 serum conferred protection against Phdp challenge, indicating that AIP56 represents a key virulence factor of that pathogen and is a candidate for the design of an anti-pasteurellosis vaccine.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.2005.04893.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Rapid and sensitive silver-lipopolysaccharide staining using PhastSystem in fast horizontal polyacrylamide gel electrophoresis (1989)
    Weinheim : Wiley-Blackwell
    Electrophoresis 10 (1989), S. 729-731 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A rapid and sensitive silver-lipopolysaccharide staining method has been developed by using PhastSystem. The total time of the procedure (including time of Phastgel electrophoresis) is within 2 h. It is at least 10 times faster than the previous reported methods and the sensitivity is also increased.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150101014
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    A novel method for specific visualisation of serum albumin in polyacrylamide gels by iodine staining (1991)
    Weinheim : Wiley-Blackwell
    Electrophoresis 12 (1991), S. 382-383 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Bovine serum, bovine serum albumins (delipidated or globulin free or Fraction V), rabbit serum, rabbit serum albumin, Atlantic salmon serum, purified Atlantic salmon serum albumin, human plasma α2-macroglobulin, hemocyanin, trypsin inhibitor, bovine transferrin and bovine lactoferrin were examined by a novel method for specific visualisation of albumins. In native polyacrylamide gel electrophoresis the albumins were visualised by iodine staining as a transparent spot against a brown background whilst the other proteins could not be visualised. It is suggested that the brown background was due to penetration of the gel by iodine while the chemical binding of iodine by albumin produced a decolourisation reaction. This novel method provides a fast and simple approach to identifying serum albumin in polyacrylamide gels.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150120513
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    Paper (German National Licenses)
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