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  • 2005-2009
  • 1980-1984  (2)
  • Pseudomonas cepacia AC1100  (1)
  • aging  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 135 (1983), S. 110-114 
    ISSN: 1432-072X
    Keywords: Emulsifying agent ; 2,4,5-Trichlorophenoxy-acetic acid ; Pseudomonas cepacia AC1100
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The culture supernatant of Pseudomonas cepacia (ATCC 39027) grown on 2,4,5-trichlorophenoxyacetic acid (2,4,5-T) was found to contain an agent which can emulsify 2,4,5-T. The emulsion is stable for several hours. The emulsifying agent was produced in response to growth on 2,4,5-T, although some emulsification was observed in culture supernatant of glucose grown cells. The emulsifying agent is most active with 2,4,5-T but has some activity towards other chlorinated compounds such as chlorophenols. In growing culture the emulsifying agent adheres to the cell surface as a slimy layer. The emulsifying agent is believed to have a role in transport of 2,4,5-T into the cells.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Basic research in cardiology 78 (1983), S. 685-694 
    ISSN: 1435-1803
    Keywords: human myosin ; ATPase ; aging ; atria ; ventricles
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Enzymatic and structural studies of human cardiac myosin from young and old subjects have been investigated to determine possible changes in myosin properties in aging hearts. Human ventricular myosin from old subjects (47–70 years old) has lower actin-activated ATPase activity than and increased alkaline sensitivity as compared to myosin from young subjects (1–132 months old). Ca2+-and K+ (EDTA)-ATPase activities, pyrophosphate gel patterns and one-dimensional peptide mapping of heavy chains of ventricular myosin from old subjects are similar to those observed for myosin from young subjects. Atrial myosin from human hearts differs significantly from ventricular myosin in that the Ca2+-, Mg2+- and actin-activated myosin Mg2+-ATPase activities of atrial myosin are significantly higher than those of ventricular myosin. Pyrophosphate gel electrophoresis patterns and peptide mapping of heavy chains of atrial myosin are also different from those of ventricular myosin. Unlike ventricular myosin, atrial myosin from young hearts is similar to that of atrial myosin from old hearts in its enzymatic and structural properties.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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