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  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Trends in Biochemical Sciences 15 (1990), S. 262-265 
    ISSN: 0968-0004
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/General Subjects 924 (1987), S. 104-110 
    ISSN: 0304-4165
    Keywords: (Bacteria) ; Bioluminescence ; Flavin intermediate ; Luciferase ; Oxygen activation
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Nuclear Instruments and Methods in Physics Research Section A: 319 (1992), S. 149-154 
    ISSN: 0168-9002
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Journal of Bioluminescence and Chemiluminescence 3 (1989), S. 79-83 
    ISSN: 0884-3996
    Keywords: Bioluminescence ; circadian rhythm ; luciferin binding protein ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A luciferin binding protein LBP involved in the bioluminescence reaction of Gonyaulax polyedra was purified and used for antibody production. Luciferin bound to LBP is fluorescent and can be used as a marker in living cells, allowing the localization of LBP in cortical organelles to be visualized. In cell sections, the same peripheral localization was observed using anti-LBP and immunofluorescence microscopy. The amount of LBP is ten-fold greater from cells from in night phase compared to those from in day phase, as determined both by immunoblots of cell extracts, and in vivo fluorescence. These changes correlate with the circadian changes in bioluminescence of living cells.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Journal of Bioluminescence and Chemiluminescence 10 (1995), S. 323-323 
    ISSN: 0884-3996
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Journal of Bioluminescence and Chemiluminescence 12 (1997), S. 15-20 
    ISSN: 0884-3996
    Keywords: bioluminescence ; bacteria ; luciferase ; superoxide anion ; dimethyl sulfoxide ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Addition of KO2 in dimethyl sulfoxide (DMSO) to the in vitro bacterial luciferase reaction subsequent to its initiation resulted in a biphasic decay of light emission. The first and more rapid phase is attributed to quenching by DMSO. With DMSO alone the continuing decay is kinetically the same as in a control reaction. With KO2 added the second decay phase is more rapid and dependent on the KO2 concentration. The enhanced decay is attributed to superoxide anion generated from KO2 reacting without light emission with an enzyme peroxy intermediate, breaking down of the peroxide bond through intermolecular electron transfer from the superoxide anion, in competiton with an intramolecular electron transfer from the N(5) position of the flavin ring, which normally leads to the production of the excited luciferase-dihydroflavin-4a-hydroxide. © 1997 John Wiley & Sons, Ltd.
    Additional Material: 4 Ill.
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  • 7
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Journal of Bioluminescence and Chemiluminescence 4 (1989), S. 12-19 
    ISSN: 0884-3996
    Keywords: Tetrapyrrole luciferin ; luc cDNA clones ; luciferase of dinoflagellates ; scintillons ; organelles ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Bioluminescence in the dinoflagellate Gonyaulax polyedra occurs as brief bright flashes, originating from many (∼400) small (∼0.5 μm) cytoplasmic organelles which protrude into the acidic vacuole, and are thus surrounded by the tonoplast. Biochemically, the substrate is unusual; it is an open chain tetrapyrrole, highly unstable to air but protected in the cell at pH̃ 8 by virtue of a luciferin binding protein (LBP). This molecule is a dimer of 72 kDa subunits which, upon a decrease in pH, releases luciferin to react with oxygen in the luciferase (∼140 kDa) catalysed luminescent reaction. cDNAs for both luciferase and LBP have been isolated and cloned, and the identity of LBP was confirmed by hybrid selection and in vitro translation of the message. The tenfold circadian (day to night) change in the amount of LBP, which parallels the in vivo rhythm of luminescence, is due to de novo synthesis and subsequent degradation of the protein each day. The LBP mRNA levels, as determined by in vitro translations and by Northern hybridizations, do not vary over the daily cycle, indicating that circadian control of bioluminescence in this species is mediated at the level of translation.
    Additional Material: 6 Ill.
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  • 8
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Journal of Bioluminescence and Chemiluminescence 4 (1989), S. 267-271 
    ISSN: 0884-3996
    Keywords: Chemiluminescence ; microtitre-plate luminometer ; opsonophagocytosis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A protocol for polymorphonuclear leukocyte chemiluminescence (PMN CL) assays of opsonophagocytosis was developed for a microtitre-plate luminometer. The complete procedure was performed in a single microtitre plate and was simpler and more efficient than previous protocols. The kinetics of the PMN CL response were best when microtitre plates were incubated on a shaking incubator between readings. The new protocol was used in a study of the pathogenicity of Corynebacterium jeikeium, an organism found in association with infection in the immunocompromised. No differences were found when PMN CL induction by 15 strains of C. jeikeium were compared with 15 isolates of other corynebacteria. Both groups of organisms required complement for efficient opsonophagocytosis; C. jeikeium strains showed no requirement for specific antibody. Resistance to opsonophagocytosis does not appear to be an explanation for the increased pathogenicity of C. jeikeium. Microtitre-plate luminometers are particularly well suited to bacterial opsonization studies where large numbers of strains often need to be assessed.
    Additional Material: 4 Ill.
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  • 9
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Journal of Bioluminescence and Chemiluminescence 4 (1989), S. 29-30 
    ISSN: 0884-3996
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Journal of Bioluminescence and Chemiluminescence 6 (1991), S. 131-136 
    ISSN: 0884-3996
    Keywords: Luciferase ; bovine serum albumin ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Bovine serum albumin (BSA) affects the amount of light obtained from bacterial luciferase by competing with luciferase for one of the luciferase substrates, the aldehyde. At low aldehyde concentrations BSA behaves as an inhibitor, but at high aldehyde concentrations BSA relieves substrate inhibition. BSA reversibly binds decanal with a Ksi = 3.36 μmol/l, approximately half the affinity of luciferase for decanal (KM = 1.5 μmol/l). BSA also increased the rate of intermediate II dark decay. The data suggest that this involves a direct protein-protein (BSA-luciferase) interaction.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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