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  • 2000-2004  (1)
  • 1990-1994  (1)
  • Amino acid sequence  (1)
  • Keywords: infrared radiation; pasteurization; antibiotic; Escherichia coli; injured cell; lethal temperature  (1)
  • 1
    Digitale Medien
    Digitale Medien
    Springer
    Journal of industrial microbiology and biotechnology 24 (2000), S. 19-24 
    ISSN: 1476-5535
    Schlagwort(e): Keywords: infrared radiation; pasteurization; antibiotic; Escherichia coli; injured cell; lethal temperature
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Escherichia coli in phosphate-buffered saline irradiated with far-infrared (FIR) energy was injured and killed even under the condition where the bulk temperature of the suspension was maintained below the lethal temperature. Using four kinds of antibiotics (penicillin G, chloramphenicol, nalidixic acid and rifampicin), we investigated the FIR irradiation-induced damage to E. coli on the basis of the sensitivity changes to the antibiotics. FIR irradiation increased the organism’s sensitivity to rifampicin both below and above the lethal temperature. The increase in sensitivity to chloramphenicol was observed only when FIR irradiation occurred above the lethal temperature. These results suggest that the mechanism of FIR irradiation-induced death in E. coli differs according to whether the radiation exposure occurs above or below the lethal temperature. Journal of Industrial Microbiology & Biotechnology (2000) 24, 19–24.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Calcified tissue international 54 (1994), S. 69-75 
    ISSN: 1432-0827
    Schlagwort(e): Porcine secretory enamel ; Porcine amelogenin ; Plasma desorption mass spectometry ; Amino acid sequence ; CNBr cleavage
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin , Physik
    Notizen: Abstract Amelogenins were extracted from the thin outer layer of porcine secretory enamel and purified by gel filtration and reverse-phase HPLC. The results of amino acid sequencing of the purified porcine amelogenins indicated the presence of at least four prototype amelogenins translated from alternatively spliced transcripts. The results of mass spectroscopy of the CNBr-cleaved peptides derived from the 25kDa amelogenin indicated that porcine 25kDa amelogenin is neither phosphorylated nor glycosylated.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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